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Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) [Cleaved into: LVV-hemorphin-7; Spinorphin]

 HBB_HUMAN               Reviewed;         147 AA.
P68871; A4GX73; B2ZUE0; P02023; Q13852; Q14481; Q14510; Q45KT0;
Q549N7; Q6FI08; Q6R7N2; Q8IZI1; Q9BX96; Q9UCD6; Q9UCP8; Q9UCP9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 163.
RecName: Full=Hemoglobin subunit beta;
AltName: Full=Beta-globin;
AltName: Full=Hemoglobin beta chain;
Contains:
RecName: Full=LVV-hemorphin-7;
Contains:
RecName: Full=Spinorphin;
Name=HBB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1019344;
Marotta C., Forget B., Cohen-Solal M., Weissman S.M.;
"Nucleotide sequence analysis of coding and noncoding regions of human
beta-globin mRNA.";
Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6254664; DOI=10.1016/0092-8674(80)90428-6;
Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.;
"The nucleotide sequence of the human beta-globin gene.";
Cell 21:647-651(1980).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-7.
PubMed=16175509; DOI=10.1086/491748;
Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.;
"The beta-globin recombinational hotspot reduces the effects of strong
selection around HbC, a recently arisen mutation providing resistance
to malaria.";
Am. J. Hum. Genet. 77:637-642(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lu L., Hu Z.H., Du C.S., Fu Y.S.;
"DNA sequence of the human beta-globin gene isolated from a healthy
Chinese.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-113.
Cabeda J.M., Correia C., Estevinho A., Cardoso C., Amorim M.L.,
Cleto E., Vale L., Coimbra E., Pinho L., Justica B.;
"Unexpected patterns of globin mutations in thalassemia patients from
north of Portugal.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LOUISVILLE LEU-43.
TISSUE=Blood;
Kutlar F., Harbin J., Brisco J., Kutlar A.;
"Rapid detection of electrophoretically silent, unstable human
hemoglobin 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA
sequencing of mRNA.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT DURHAM-N.C. PRO-115.
TISSUE=Blood;
Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.;
"Electrophoretically silent, very unstable, thalassemic mutation at
codon 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA
sequencing of mRNA, from a Russian women.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TY GARD GLN-125.
TISSUE=Blood;
Kutlar F., Holley L., Leithner C., Kutlar A.;
"A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a
Caucasian female with erythrocytosis.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D.,
Kutlar F.;
"Heterozygote C->A beta-thalassemia mutation at the intron-2/848
nucleotide of beta globin gene was detected on a Northern European
(Caucasian) individual.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT SKCA VAL-7, AND VARIANT SER-140.
TISSUE=Blood;
Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.;
"A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on
the same chromosome with hemoglobin S mutation, detected in an
African-American family.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT O-ARAB LYS-122.
TISSUE=Blood;
Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.;
"Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta-
thalassemia (intron-2; nucleotide 745 C->G) was detected in a Turkish
patient.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Li W.J.;
"Thalassaemic trait cause by C-T substitution at position -90 in
proximal CACCC box of beta-globin gene in China family.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PHE-50 AND PRO-76.
TISSUE=Lymphocyte;
Fan B., Xie L., Guan X.;
"The differently expressed genes in the lymphocyte of recovered SARS
patients.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
Mehta S., Li T., Davis D.H., Nechtman J., Kutlar F.;
"Beta-thalassemia G->C mutation at the nucleotide 5 position of intron
1 of beta globin gene was detected in Asian-Indian female with two
polymorphisms in cis.";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA].
Hilliard L.M., Patel N., Li T., Zhang H., Kutlar A., Kutlar F.;
"Hb Dothan: a novel beta chain variant due to (-GTG) deletion between
the codons 25/26 of beta globin gene detected in a Caucasian male
baby.";
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[19]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[20]
PROTEIN SEQUENCE OF 2-147.
PubMed=13872627; DOI=10.1515/bchm2.1961.325.1.283;
Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
Rudloff V., Wittmann-Liebold B.;
"The constitution of normal adult human haemoglobin.";
Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
[21]
PROTEIN SEQUENCE OF 3-9, INVOLVEMENT IN SKCA, AND VARIANT SKCA VAL-7.
PubMed=13464827; DOI=10.1038/180326a0;
Ingram V.M.;
"Gene mutations in human haemoglobin: the chemical difference between
normal and sickle cell haemoglobin.";
Nature 180:326-328(1957).
[22]
PROTEIN SEQUENCE OF 19-31, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Tear;
PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
Suarez T., Elortza F.;
"Human basal tear peptidome characterization by CID, HCD, and ETD
followed by in silico and in vitro analyses for antimicrobial peptide
identification.";
J. Proteome Res. 14:2649-2658(2015).
[23]
PROTEIN SEQUENCE OF 33-42, AND MASS SPECTROMETRY.
PubMed=1575724; DOI=10.1016/0006-291X(92)90699-L;
Glaemsta E.-L., Meyerson B., Silberring J., Terenius L., Nyberg F.;
"Isolation of a hemoglobin-derived opioid peptide from cerebrospinal
fluid of patients with cerebrovascular bleedings.";
Biochem. Biophys. Res. Commun. 184:1060-1066(1992).
[24]
PROTEIN SEQUENCE OF 33-42.
Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S.,
de Camargo A.C.M., Pimenta D.C.;
Submitted (JUN-2007) to UniProtKB.
[25]
PROTEIN SEQUENCE OF 97-121, NUCLEOTIDE SEQUENCE [MRNA] OF 106-113, AND
VARIANT BURKE ARG-108.
PubMed=8401300;
Suzuki H., Wada C., Kamata K., Takahashi E., Sato N., Kunitomo T.;
"Globin chain synthesis in hemolytic anemia reticulocytes. A case of
hemoglobin Burke.";
Biochem. Mol. Biol. Int. 30:425-431(1993).
[26]
NUCLEOTIDE SEQUENCE [MRNA] OF 122-147.
PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9;
Lang K.M., Spritz R.A.;
"Cloning specific complete polyadenylylated 3'-terminal cDNA
segments.";
Gene 33:191-196(1985).
[27]
BISPHOSPHOGLYCERATE BINDING.
PubMed=4555506; DOI=10.1038/237146a0;
Arnone A.;
"X-ray diffraction study of binding of 2,3-diphosphoglycerate to human
deoxyhaemoglobin.";
Nature 237:146-149(1972).
[28]
ACETYLATION AT LYS-60; LYS-83 AND LYS-145.
PubMed=4531009; DOI=10.1073/pnas.71.12.4693;
Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.;
"Sites of acetylation of sickle cell hemoglobin by aspirin.";
Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974).
[29]
GLYCATION AT VAL-2.
PubMed=635569; DOI=10.1126/science.635569;
Bunn H.F., Gabbay K.H., Gallop P.M.;
"The glycosylation of hemoglobin: relevance to diabetes mellitus.";
Science 200:21-27(1978).
[30]
GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, AND LACK OF
GLYCATION AT LYS-60; LYS-83 AND LYS-96.
PubMed=7358733;
Shapiro R., McManus M.J., Zalut C., Bunn H.F.;
"Sites of nonenzymatic glycosylation of human hemoglobin A.";
J. Biol. Chem. 255:3120-3127(1980).
[31]
INVOLVEMENT IN B-THAL, AND VARIANT B-THAL LYS-27.
PubMed=6166632; DOI=10.1172/JCI110226;
Benz E.J. Jr., Berman B.W., Tonkonow B.L., Coupal E., Coates T.,
Boxer L.A., Altman A., Adams J.G. III;
"Molecular analysis of the beta-thalassemia phenotype associated with
inheritance of hemoglobin E (alpha 2 beta2(26)Glu leads to Lys).";
J. Clin. Invest. 68:118-126(1981).
[32]
SUBUNIT, TISSUE SPECIFICITY, AND PARTIAL PROTEIN SEQUENCE.
PubMed=6539334;
Randhawa Z.I., Jones R.T., Lie-Injo L.E.;
"Human hemoglobin Portland II (zeta 2 beta 2). Isolation and
characterization of Portland hemoglobin components and their
constituent globin chains.";
J. Biol. Chem. 259:7325-7330(1984).
[33]
INTERACTION WITH HAPTOGLOBIN.
PubMed=3718478; DOI=10.1042/bj2340453;
Yoshioka N., Atassi M.Z.;
"Haemoglobin binding with haptoglobin. Localization of the
haptoglobin-binding sites on the beta-chain of human haemoglobin by
synthetic overlapping peptides encompassing the entire chain.";
Biochem. J. 234:453-456(1986).
[34]
MODIFICATION AT LEU-142.
PubMed=1520632; DOI=10.1111/j.1365-2141.1992.tb08179.x;
Brennan S.O., Shaw J., Allen J., George P.M.;
"Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-
Coventry but is replaced by a novel amino acid of mass 129 daltons.";
Br. J. Haematol. 81:99-103(1992).
[35]
S-NITROSYLATION AT CYS-94.
PubMed=8637569; DOI=10.1038/380221a0;
Jia L., Bonaventura C., Bonaventura J., Stamler J.S.;
"S-nitrosohaemoglobin: a dynamic activity of blood involved in
vascular control.";
Nature 380:221-226(1996).
[36]
S-NITROSYLATION AT CYS-94.
PubMed=9843411; DOI=10.1021/bi9816711;
Chan N.L., Rogers P.H., Arnone A.;
"Crystal structure of the S-nitroso form of liganded human
hemoglobin.";
Biochemistry 37:16459-16464(1998).
[37]
NITRIC OXIDE-BINDING.
PubMed=10588683; DOI=10.1073/pnas.96.25.14206;
Durner J., Gow A.J., Stamler J.S., Glazebrook J.;
"Ancient origins of nitric oxide signaling in biological systems.";
Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999).
[38]
POLYMORPHISM, AND ASSOCIATION OF VARIANT LYS-7 WITH RESISTANCE TO
MALARIA.
PubMed=11001883;
Agarwal A., Guindo A., Cissoko Y., Taylor J.G., Coulibaly D., Kone A.,
Kayentao K., Djimde A., Plowe C.V., Doumbo O., Wellems T.E.,
Diallo D.;
"Hemoglobin C associated with protection from severe malaria in the
Dogon of Mali, a West African population with a low prevalence of
hemoglobin S.";
Blood 96:2358-2363(2000).
[39]
SUBUNIT.
PubMed=11747442; DOI=10.1021/bi011329f;
Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.;
"The role of beta chains in the control of the hemoglobin oxygen
binding function: chimeric human/mouse proteins, structure, and
function.";
Biochemistry 40:15669-15675(2001).
[40]
POLYMORPHISM, AND ASSOCIATION OF VARIANT B-THAL LYS-27 WITH RESISTANCE
TO MALARIA.
PubMed=12149194;
Chotivanich K., Udomsangpetch R., Pattanapanyasat K., Chierakul W.,
Simpson J., Looareesuwan S., White N.;
"Hemoglobin E: a balanced polymorphism protective against high
parasitemias and thus severe P falciparum malaria.";
Blood 100:1172-1176(2002).
[41]
REVIEW ON FUNCTION OF SPINORPHIN.
PubMed=12470213; DOI=10.2174/1389203023380404;
Yamamoto Y., Ono H., Ueda A., Shimamura M., Nishimura K., Hazato T.;
"Spinorphin as an endogenous inhibitor of enkephalin-degrading
enzymes: roles in pain and inflammation.";
Curr. Protein Pept. Sci. 3:587-599(2002).
[42]
POLYMORPHISM, AND ASSOCIATION OF VARIANT SKCA VAL-7 WITH RESISTANCE TO
MALARIA.
PubMed=16001361; DOI=10.1086/432519;
Kwiatkowski D.P.;
"How malaria has affected the human genome and what human genetics can
teach us about malaria.";
Am. J. Hum. Genet. 77:171-192(2005).
[43]
SYNTHESIS OF 33-42, AND FUNCTION.
PubMed=16904236; DOI=10.1016/j.peptides.2006.06.009;
Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S.,
de Camargo A.C.M., Pimenta D.C.;
"Hemorphin and hemorphin-like peptides isolated from dog pancreas and
sheep brain are able to potentiate bradykinin activity in vivo.";
Peptides 27:2957-2966(2006).
[44]
FUNCTION OF SPINORPHIN.
PubMed=17676725; DOI=10.1021/jm070114m;
Jung K.Y., Moon H.D., Lee G.E., Lim H.H., Park C.S., Kim Y.C.;
"Structure-activity relationship studies of spinorphin as a potent and
selective human P2X(3) receptor antagonist.";
J. Med. Chem. 50:4543-4547(2007).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-13; SER-45;
THR-51 AND THR-88, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[47]
ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS.
PubMed=4123689; DOI=10.1073/pnas.70.3.718;
Finch J.T., Perutz M.F., Bertles J.F., Doebler J.;
"Structure of sickled erythrocytes and of sickle-cell hemoglobin
fibers.";
Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973).
[48]
X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF VARIANT SKCA VAL-7.
PubMed=1195378; DOI=10.1016/S0022-2836(75)80108-2;
Wishner B.C., Ward K.B., Lattman E.E., Love W.E.;
"Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution.";
J. Mol. Biol. 98:179-194(1975).
[49]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4;
Fermi G.;
"Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5-
A resolution: refinement of the atomic model.";
J. Mol. Biol. 97:237-256(1975).
[50]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN.
PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
Baldwin J.M.;
"The structure of human carbonmonoxy haemoglobin at 2.7-A
resolution.";
J. Mol. Biol. 136:103-128(1980).
[51]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN.
PubMed=6726807; DOI=10.1016/0022-2836(84)90472-8;
Fermi G., Perutz M.F., Shaanan B., Fourme R.;
"The crystal structure of human deoxyhaemoglobin at 1.74 A
resolution.";
J. Mol. Biol. 175:159-174(1984).
[52]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38.
PubMed=1567857; DOI=10.1021/bi00131a030;
Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.;
"High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta
Trp-->Arg: a mutation that creates an intersubunit chloride-binding
site.";
Biochemistry 31:4111-4121(1992).
[53]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75.
PubMed=1507231; DOI=10.1016/0022-2836(92)90638-Z;
Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.;
"Structure-function relationships in the low-affinity mutant
haemoglobin Aalborg (Gly74 (E18)beta-->Arg).";
J. Mol. Biol. 226:883-888(1992).
[54]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND BISPHOSPHOGLYCERATE
BINDING.
PubMed=8377203; DOI=10.1006/jmbi.1993.1505;
Richard V., Dodson G.G., Mauguen Y.;
"Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt
structure at 2.5 A resolution.";
J. Mol. Biol. 233:270-274(1993).
[55]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=8642597; DOI=10.1006/jmbi.1996.0124;
Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.;
"Crystal structure of T state haemoglobin with oxygen bound at all
four haems.";
J. Mol. Biol. 256:775-792(1996).
[56]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38;
GLY-38 AND TYR-38.
PubMed=9521756; DOI=10.1021/bi9708702;
Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.;
"High-resolution crystal structures of human hemoglobin with mutations
at tryptophan 37beta: structural basis for a high-affinity T-state.";
Biochemistry 37:4358-4373(1998).
[57]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7.
PubMed=9830011; DOI=10.1074/jbc.273.49.32690;
Harrington D.J., Adachi K., Royer W.E. Jr.;
"Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp.
Implications for the structure and formation of the sickle cell
fiber.";
J. Biol. Chem. 273:32690-32696(1998).
[58]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANT LYS-7.
PubMed=12454462; DOI=10.1107/S0907444902016426;
Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L.,
Patskovsky Y., Nagel R.L., Almo S.C., Hirsch R.E.;
"Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A
resolution.";
Acta Crystallogr. D 58:2038-2042(2002).
[59]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF VARIANT SKCA VAL-7 IN
COMPLEX WITH HEME AND HBZ, AND SUBUNIT.
PubMed=24100324; DOI=10.1107/S0907444913019197;
Safo M.K., Ko T.P., Abdulmalik O., He Z., Wang A.H., Schreiter E.R.,
Russell J.E.;
"Structure of fully liganded Hb zeta2beta2s trapped in a tense
conformation.";
Acta Crystallogr. D 69:2061-2071(2013).
[60]
VARIANT FREIBURG VAL-24 DEL.
PubMed=5919752; DOI=10.1126/science.154.3752.1024;
Jones R.T., Brimhall B., Huisman T.H., Kleihauer E., Betke K.;
"Hemoglobin Freiburg: abnormal hemoglobin due to deletion of a single
amino acid residue.";
Science 154:1024-1027(1966).
[61]
VARIANT ALABAMA LYS-40.
PubMed=1115799;
Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G.,
Atkins R.;
"Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
Biochim. Biophys. Acta 379:28-32(1975).
[62]
INVOLVEMENT IN HEIBAN, AND VARIANT ST LOUIS GLN-29.
PubMed=186485; DOI=10.1172/JCI108561;
Thillet J., Cohen-Solal M., Seligmann M., Rosa J.;
"Functional and physicochemical studies of hemoglobin St. Louis beta
28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron.";
J. Clin. Invest. 58:1098-1106(1976).
[63]
INVOLVEMENT IN B-THALIB.
PubMed=1971109; DOI=10.1073/pnas.87.10.3924;
Thein S.L., Hesketh C., Taylor P., Temperley I.J., Hutchinson R.M.,
Old J.M., Wood W.G., Clegg J.B., Weatherall D.J.;
"Molecular basis for dominantly inherited inclusion body beta-
thalassemia.";
Proc. Natl. Acad. Sci. U.S.A. 87:3924-3928(1990).
[64]
VARIANT ALESHA MET-68.
PubMed=8330974; DOI=10.3109/03630269308998896;
Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S.,
Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.;
"Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable
hemoglobin variant identified through sequencing of amplified DNA.";
Hemoglobin 17:217-225(1993).
[65]
VARIANT J-ALTGELDS GARDENS ASP-93.
PubMed=721609; DOI=10.3109/03630267809007075;
Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.;
"Hemoglobin J Altgeld Gardens. A hemoglobin variant with a
substitution of the proximal histidine of the beta-chain.";
Hemoglobin 2:403-415(1978).
[66]
VARIANT ANKARA ASP-11.
PubMed=4850241; DOI=10.1016/0014-5793(74)80766-0;
Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.;
"A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp).";
FEBS Lett. 42:121-123(1974).
[67]
VARIANT J-ANTAKYA MET-66, AND VARIANT COMPLUTENSE GLU-128.
PubMed=3707969; DOI=10.1016/0167-4838(86)90178-0;
Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S.,
Webber B.B., Altay C., Martinez A.V.;
"Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family
and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish
family; correction of a previously published identification.";
Biochim. Biophys. Acta 871:229-231(1986).
[68]
VARIANT J-AUCKLAND ASP-26.
PubMed=3654265; DOI=10.3109/03630268709017888;
Williamson D., Wells R.M.G., Anderson R., Matthews J.;
"A new unstable and low oxygen affinity hemoglobin variant: Hb J-
Auckland [beta 25(B7)Gly-->Asp].";
Hemoglobin 11:221-230(1987).
[69]
VARIANT AURORA TYR-140.
PubMed=8718692; DOI=10.3109/03630269509005825;
Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.;
"Identification of a new high oxygen affinity hemoglobin variant: Hb
Aurora [beta 139(H17) Asn-->Tyr].";
Hemoglobin 19:335-341(1995).
[70]
VARIANT BREST LYS-128.
PubMed=3384710; DOI=10.3109/03630268808998024;
Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J.,
Briere J., Galacteros F.;
"Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human
hemoglobin variant located at the alpha 1 beta 1 interface with
specific electrophoretic behavior.";
Hemoglobin 12:179-188(1988).
[71]
VARIANT BRISBANE HIS-69.
PubMed=6166590; DOI=10.3109/03630268108991807;
Brennan S.O., Wells R.M., Smith H., Carrell R.W.;
"Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen
affinity variant.";
Hemoglobin 5:325-335(1981).
[72]
VARIANT BUNBURY ASN-95.
PubMed=6629823; DOI=10.3109/03630268309038410;
Como P.F., Kennett D., Wilkinson T., Kronenberg H.;
"A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury:
alpha 2 beta 2 [94 (FG1) Asp replaced by Asn].";
Hemoglobin 7:413-421(1983).
[73]
VARIANT J-CAIRO GLN-66.
PubMed=1247583;
Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.;
"Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin
variant discovered in an Egyptian family.";
Biochim. Biophys. Acta 420:97-104(1976).
[74]
VARIANT CAMPERDOWN SER-105.
PubMed=1138922;
Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M.,
Kronenberg H.;
"A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6)
arginine->serine).";
Biochim. Biophys. Acta 393:195-200(1975).
[75]
VARIANT CARIBBEAN ARG-92.
PubMed=992050; DOI=10.1016/0014-5793(76)80662-X;
Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E.,
Seakins M., Lang A., Middleton A., Lehmann H.;
"Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly
haemoglobin with a low oxygen affinity.";
FEBS Lett. 69:99-102(1976).
[76]
VARIANT CITY OF HOPE SER-70.
PubMed=6434492; DOI=10.3109/03630268408991716;
Rahbar S., Asmerom Y., Blume K.G.;
"A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope
beta 69 (E13) Gly-->Ser.";
Hemoglobin 8:333-342(1984).
[77]
VARIANT COIMBRA GLU-100.
PubMed=1814856; DOI=10.3109/03630269109027896;
Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M.,
Wilson J.B., Baysal E., Gu L.H., Huisman T.H.J.;
"Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered
high oxygen affinity variant.";
Hemoglobin 15:487-496(1991).
[78]
VARIANT COSTA RICA ARG-78.
PubMed=8641705; DOI=10.1007/BF02346198;
Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H.,
Wilson J.B., Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.;
"Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example
of a somatic cell mutation in a globin gene.";
Hum. Genet. 97:829-833(1996).
[79]
VARIANT DEBROUSSE PRO-97.
PubMed=8602627;
DOI=10.1002/(SICI)1096-8652(199604)51:4<276::AID-AJH5>3.0.CO;2-T;
Lacan P., Kister J., Francina A., Souillet G., Galacteros F.,
Delaunay J., Wajcman H.;
"Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable
hemoglobin with twofold increased oxygen affinity.";
Am. J. Hematol. 51:276-281(1996).
[80]
VARIANT B-THAL GLY-127.
PubMed=2399911; DOI=10.1002/ajh.2830350206;
Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J.,
Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P.,
Galacteros F.;
"Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable
beta variant producing a beta-thalassemia intermedia phenotype in
association with beta zero-thalassemia.";
Am. J. Hematol. 35:96-99(1990).
[81]
VARIANT NEWCASTLE PRO-93, VARIANT CAMPERDOWN SER-105, AND DESCRIPTION
OF VARIANT DUINO.
PubMed=1511986; DOI=10.1007/BF00221961;
Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
Melevendi C., Rasore A., Galacteros F.;
"Two new human hemoglobin variants caused by unusual mutational
events: Hb Zaire contains a five residue repetition within the alpha-
chain and Hb Duino has two residues substituted in the beta-chain.";
Hum. Genet. 89:676-680(1992).
[82]
VARIANT DURHAM-N.C. PRO-115.
PubMed=1301199; DOI=10.1002/humu.1380010207;
Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M.,
Melevendi C., Pirastu M., Cao A.;
"A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro),
causing a severe beta-thalassemia intermedia phenotype.";
Hum. Mutat. 1:124-128(1992).
[83]
VARIANT DURHAM-N.C. PRO-115.
PubMed=8111050;
de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.;
"A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro],
produces a dominant thalassemia-like phenotype.";
Blood 83:1109-1116(1994).
[84]
VARIANT J-EUROPA ASP-63.
PubMed=8811317; DOI=10.3109/03630269609027919;
Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F.,
Wajcman H.;
"Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties
in a new variant involving a residue located distal to the heme.";
Hemoglobin 20:135-140(1996).
[85]
VARIANT GEELONG ASP-140.
PubMed=1917539; DOI=10.3109/03630269109072487;
Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B.,
Tibben E.A., Wilkinson T., Kronenberg H.;
"Hb Geelong [beta 139(H17)Asn-->Asp].";
Hemoglobin 15:85-95(1991).
[86]
VARIANT GRANGE-BLANCHE VAL-28.
PubMed=3666141; DOI=10.1016/0014-5793(87)80509-4;
Baklouti F., Giraud Y., Francina A., Richard G., Perier C.,
Geyssant A., Jaubert J., Brizard C., Delaunay J.;
"Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with
normal expression and increased affinity for oxygen.";
FEBS Lett. 223:59-62(1987).
[87]
VARIANT GRAZ LEU-3.
PubMed=1487420; DOI=10.3109/03630269208993117;
Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P.,
Schnedl W., Balaun E., Krejs G.J., Huisman T.H.J.;
"Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant
observed in four families from southern Austria.";
Hemoglobin 16:493-501(1992).
[88]
VARIANT HELSINKI MET-83.
PubMed=826083;
Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F.,
Nagai K., Lang A., Lehmann H.;
"Hb Helsinki: a variant with a high oxygen affinity and a substitution
at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met).";
Acta Haematol. 56:257-275(1976).
[89]
VARIANT HIMEJI ASP-141.
PubMed=3754244; DOI=10.3109/03630268609046438;
Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M.,
Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.;
"Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin
with increased beta N-terminal glycation.";
Hemoglobin 10:109-126(1986).
[90]
VARIANT HINSDALE LYS-140.
PubMed=2513289; DOI=10.3109/03630268908998084;
Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.;
"Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central
cavity showing reduced affinity for oxygen and 2,3-
diphosphoglycerate.";
Hemoglobin 13:455-464(1989).
[91]
VARIANT HINWIL ASN-39.
PubMed=8745430; DOI=10.3109/03630269609027908;
Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C.,
Cao A., Breitenstein U., Fehr J., Tuchschmid P.;
"HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected
in a Swiss family.";
Hemoglobin 20:31-40(1996).
[92]
VARIANT HOWICK GLY-38.
PubMed=8144352; DOI=10.3109/03630269309043491;
Owen M.C., Ockelford P.A., Wells R.M.G.;
"Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant
of the alpha 1 beta 2 contact.";
Hemoglobin 17:513-521(1993).
[93]
VARIANT INDIANAPOLIS ARG-113.
PubMed=429365;
Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G.,
Tsistrakis G.A.;
"The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An
unstable variant detectable only by isotopic labeling.";
J. Biol. Chem. 254:3479-3482(1979).
[94]
VARIANT ISEHARA ASN-93.
PubMed=1787097; DOI=10.3109/03630269109027880;
Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.;
"Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable
variant with a proximal histidine substitution at the heme contact.";
Hemoglobin 15:279-290(1991).
[95]
VARIANT ISTAMBUL GLN-93.
PubMed=4639022; DOI=10.1172/JCI107050;
Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J.,
Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.;
"Hemoglobin Istanbul: substitution of glutamine for histidine in a
proximal histidine (F8(92)).";
J. Clin. Invest. 51:2380-2387(1972).
[96]
VARIANT JACKSONVILLE ASP-55.
PubMed=2101840;
Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H.,
Moo-Penn W.F.;
"Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable
variant found in a patient with hemolytic anemia.";
Hemoglobin 14:653-659(1990).
[97]
VARIANT JIANGHUA ILE-121.
PubMed=6618888;
Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H.,
Huang P.Y., Chen S.S., Jai P.C., Yang K.G.;
"Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast-
moving variant found in China.";
Hemoglobin 7:321-326(1983).
[98]
VARIANT KARLSKOGA HIS-22.
PubMed=8330972; DOI=10.3109/03630269308998894;
Landin B.;
"Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving
variant found in Sweden.";
Hemoglobin 17:201-208(1993).
[99]
VARIANT KNOSSOS SER-28.
PubMed=7173395; DOI=10.1016/0014-5793(82)81052-1;
Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y.,
Komis G., Sellaye M., Boussiou M., Rosa J.;
"Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to
Ser. A new abnormal hemoglobin present as a silent beta-thalassemia.";
FEBS Lett. 147:247-250(1982).
[100]
VARIANT KODAIRA GLN-147.
PubMed=1634367; DOI=10.3109/03630269209005681;
Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R.,
Matsunaga T.;
"Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an
amino acid substitution at the C-terminus.";
Hemoglobin 16:85-91(1992).
[101]
VARIANT KOFU ILE-85.
PubMed=3744871; DOI=10.3109/03630268608996871;
Harano T., Harano K., Ueda S., Imai N., Kitazumi T.;
"A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu
or alpha 2 beta 2 84 (EF8) Thr-->Ile.";
Hemoglobin 10:417-420(1986).
[102]
VARIANT B-THAL ASP-116.
PubMed=7693620; DOI=10.3109/03630269308997485;
Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P.,
Huisman T.H.J.;
"Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a
severely unstable hemoglobin variant resulting in a dominant beta-
thalassemia trait in a Czech family.";
Hemoglobin 17:319-328(1993).
[103]
VARIANT LA DESIRADE VAL-130.
PubMed=3557994; DOI=10.3109/03630268609036564;
Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N.,
Galacteros F., Feingold J., Rosa J.;
"Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new
unstable hemoglobin.";
Hemoglobin 10:593-605(1986).
[104]
VARIANT LA ROCHE-SUR-YON HIS-82.
PubMed=1540659; DOI=10.1016/0925-4439(92)90052-O;
Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C.,
Cottenceau D., Galacteros F.;
"Structure of the EF corner favors deamidation of asparaginyl residues
in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5)
Leu-->His].";
Biochim. Biophys. Acta 1138:127-132(1992).
[105]
VARIANT LAS PALMAS PHE-50.
PubMed=3384708; DOI=10.3109/03630268808998022;
Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H.,
Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.;
"Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable
hemoglobin variant.";
Hemoglobin 12:163-170(1988).
[106]
VARIANT LINKOPING THR-37.
PubMed=3691763;
Berlin G., Wranne B., Jeppsson J.-O.;
"Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity
hemoglobin variant found in two families of Finnish origin.";
Eur. J. Haematol. 39:452-456(1987).
[107]
VARIANT MAPUTO TYR-48.
PubMed=6629824; DOI=10.3109/03630268309038411;
Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L.,
Labie D.;
"Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6)
Asp replaced by Tyr) in combination with hemoglobin S, identified by
high performance liquid chromatography (HPLC).";
Hemoglobin 7:423-433(1983).
[108]
VARIANT MATERA LYS-56.
PubMed=2384314; DOI=10.3109/03630269009002256;
Sciarratta G.V., Ivaldi G.;
"Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant
in an Italian family.";
Hemoglobin 14:79-85(1990).
[109]
VARIANT MIYASHIRO GLY-24.
PubMed=7338468; DOI=10.3109/03630268108991833;
Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H.,
Shinohara T., Hori T., Takayama J.;
"Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an
electrophoretically silent variant discovered by the isopropanol
test.";
Hemoglobin 5:653-666(1981).
[110]
VARIANT MIZUHO PRO-69.
PubMed=893142; DOI=10.3109/03630267709027864;
Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.;
"Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new
unstable variant associated with severe hemolytic anemia.";
Hemoglobin 1:467-477(1977).
[111]
VARIANT MUSCAT VAL-33.
PubMed=1517102; DOI=10.3109/03630269208998866;
Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D.,
Liu J.C., McKie K.M., Huisman T.H.J.;
"A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed
in association with HB S in an Arabian family.";
Hemoglobin 16:259-266(1992).
[112]
VARIANT N-TIMONE GLU-9.
PubMed=2634671; DOI=10.3109/03630268908998848;
Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C.,
Blouquit Y., Craescu C.T., Galacteros F.;
"Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving
variant with normal stability and oxygen affinity.";
Hemoglobin 13:743-747(1989).
[113]
VARIANT NAGOYA PRO-98.
PubMed=3838976; DOI=10.3109/03630268508996978;
Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C.,
Shibata K., Shimokata H., Kuzuya F., Miwa S.;
"A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97
(FG4) His-->Pro.";
Hemoglobin 9:11-24(1985).
[114]
VARIANT D-NEATH ALA-122.
PubMed=8330979; DOI=10.3109/03630269308998901;
Welch S.G., Bateman C.;
"Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D
family.";
Hemoglobin 17:255-259(1993).
[115]
VARIANT NORTH CHICAGO SER-37.
PubMed=3937824; DOI=10.3109/03630268508997038;
Rahbar S., Louis J., Lee T., Asmerom Y.;
"Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high
affinity hemoglobin.";
Hemoglobin 9:559-576(1985).
[116]
VARIANT NORTH SHORE-CARACAS GLU-135.
PubMed=891976; DOI=10.1016/0014-5793(77)80453-5;
Arends T., Lehmann H., Plowman D., Stathopoulou R.;
"Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by
glutamic acid.";
FEBS Lett. 80:261-265(1977).
[117]
VARIANT OLOMOUC ASP-87.
PubMed=3623975; DOI=10.3109/03630268709005790;
Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B.,
Kutlar A., Huisman T.H.J.;
"Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen
affinity variant.";
Hemoglobin 11:151-155(1987).
[118]
VARIANT PALMERSTON NORTH PHE-24.
PubMed=7161106; DOI=10.3109/03630268209046450;
Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.;
"Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new
variant identified in a patient with polycythemia.";
Hemoglobin 6:569-575(1982).
[119]
VARIANT PIERRE-BENITE ASP-91.
PubMed=3384709; DOI=10.3109/03630268808998023;
Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J.,
Delaunay J.;
"Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity
variant found in a French family.";
Hemoglobin 12:171-177(1988).
[120]
VARIANT PRESBYTERIAN LYS-109.
PubMed=668922; DOI=10.1016/0014-5793(78)80720-0;
Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.;
"Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A
hemoglobin variant with low oxygen affinity.";
FEBS Lett. 92:53-56(1978).
[121]
VARIANT PUTTELANGE VAL-141.
PubMed=8522332; DOI=10.1007/BF00210304;
Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I.,
Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J.,
Goossens M., Galacteros F.;
"Germline mosaicism for an alanine to valine substitution at residue
beta 140 in hemoglobin Puttelange, a new variant with high oxygen
affinity.";
Hum. Genet. 96:711-716(1995).
[122]
VARIANT QUIN-HAI ARG-79.
PubMed=6629822; DOI=10.3109/03630268309038409;
Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y.,
Chang F.Q., Chow Y.C., Chiu Y.;
"Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new
abnormal hemoglobin found in Guangdong, China.";
Hemoglobin 7:407-412(1983).
[123]
VARIANT RAMBAM ASP-70.
PubMed=9761252;
Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W.,
van Dorsselaer A., Wieland H.;
"Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment
of diabetic control: characterization by electrospray mass
spectrometry and HPLC.";
Clin. Chem. 44:2172-2177(1998).
[124]
VARIANT RANDWICK GLY-16.
PubMed=3384707; DOI=10.3109/03630268808998021;
Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F.,
Kwan Y.L., Holland R.A.B.;
"Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta-
chain hemoglobin variant.";
Hemoglobin 12:149-161(1988).
[125]
VARIANT RIO GRANDE THR-9.
PubMed=6857757; DOI=10.3109/03630268309038405;
Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.,
Therrell B.L. Jr.;
"Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant
found in a Mexican-American family.";
Hemoglobin 7:91-95(1983).
[126]
VARIANT RUSH GLN-102.
PubMed=4129558;
Adams J.G. III, Winter W.P., Tausk K., Heller P.;
"Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin
causing mild hemolytic anemia.";
Blood 43:261-269(1974).
[127]
VARIANT SAITAMA PRO-118.
PubMed=6687721; DOI=10.3109/03630268309038400;
Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y.,
Miyaji T.;
"Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant
causing hemolytic disease.";
Hemoglobin 7:47-56(1983).
[128]
VARIANT M-SASKATOON TYR-64.
PubMed=13897827; DOI=10.1073/pnas.47.11.1758;
Gerald P.S., Efron M.L.;
"Chemical studies of several varieties of Hb M.";
Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961).
[129]
VARIANT SHELBY/LESLIE/DEACONESS LYS-132.
PubMed=6526653; DOI=10.3109/03630268408991743;
Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.;
"Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the
structure of hemoglobin Deaconess and hemoglobin Leslie.";
Hemoglobin 8:583-593(1984).
[130]
VARIANT J-SICILIA ASN-66.
PubMed=4852224; DOI=10.1016/0014-5793(74)80050-5;
Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.;
"Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia.";
FEBS Lett. 39:200-204(1974).
[131]
VARIANT STANMORE ALA-112.
PubMed=1917537; DOI=10.3109/03630269109072484;
Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T.,
Kronenberg H., Holland R.A.B., Tibben E.A.;
"A new unstable and low oxygen affinity hemoglobin variant: Hb
Stanmore [beta 111(G13)Val-->Ala].";
Hemoglobin 15:53-65(1991).
[132]
VARIANT ST MANDE TYR-103.
PubMed=7238856; DOI=10.1016/0014-5793(81)81046-0;
Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F.,
Chevrier M., Bordahandy C., Rosa J.;
"Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low
oxygen affinity variant.";
FEBS Lett. 126:114-116(1981).
[133]
VARIANT WINDSOR ASP-12.
PubMed=2599880; DOI=10.3109/03630268908998083;
Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B.,
Tibben E.A.;
"Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta-
chain hemoglobin variant producing a hemolytic anemia.";
Hemoglobin 13:437-453(1989).
[134]
VARIANT YAHATA TYR-113.
PubMed=1917530; DOI=10.3109/03630269109072490;
Harano T., Harano K., Kushida Y., Ueda S.;
"A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in
a Japanese: structural confirmation by DNA sequencing of the beta-
globin gene.";
Hemoglobin 15:109-113(1991).
[135]
VARIANT YOKOHAMA PRO-32.
PubMed=7338469; DOI=10.3109/03630268108991834;
Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S.,
Matsumoto N.;
"A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting
for Pro, causing hemolytic anemia.";
Hemoglobin 5:667-678(1981).
[136]
INVOLVEMENT IN HEIBAN, AND VARIANT HAMMERSMITH SER-43.
PubMed=6259091; DOI=10.3109/03630268108996914;
Rahbar S., Feagler R.J., Beutler E.;
"Hemoglobin Hammersmith (beta 42 (CD1) Phe replaced by Ser) associated
with severe hemolytic anemia.";
Hemoglobin 5:97-105(1981).
[137]
INVOLVEMENT IN HEIBAN, AND VARIANTS BRUXELLES PHE-42 DEL AND PHE-43
DEL.
PubMed=2599881; DOI=10.3109/03630268908998085;
Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H.,
Orsini A., Rosa J., Galacteros F.;
"Hb Bruxelles: alpha 2A beta (2)41 or 42(C7 or CD1)Phe deleted.";
Hemoglobin 13:465-474(1989).
[138]
VARIANT ZENGCHENG MET-115.
PubMed=2079435; DOI=10.3109/03630269009005808;
Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J.,
Zeng Y.T., Shen M.;
"Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met.";
Hemoglobin 14:555-557(1990).
[139]
VARIANT BECKMAN ASP-136.
Rahbar S., Lee T., Asmeron Y.;
"Hb Beckman alpha135 (H13) ala-to-glu: a new unstable variant and
reduced oxygen affinity.";
Blood 78:204A-204A(1991).
[140]
VARIANT NON-SPHEROCYTIC HAEMOLITIC ANEMIA GLY-68.
PubMed=8280608; DOI=10.1111/j.1365-2141.1993.tb03178.x;
Fay K.C., Brennan S.O., Costello J.M., Potter H.C., Williamson D.A.,
Trent R.J., Ockelford P.A., Boswell D.R.;
"Haemoglobin Manukau beta 67[E11] Val-->Gly: transfusion-dependent
haemolytic anaemia ameliorated by coexisting alpha thalassaemia.";
Br. J. Haematol. 85:352-355(1993).
[141]
INVOLVEMENT IN HEIBAN, AND VARIANT BRISTOL ASP-68.
PubMed=8704193;
Rees D.C., Rochette J., Schofield C., Green B., Morris M.,
Parker N.E., Sasaki H., Tanaka A., Ohba Y., Clegg J.B.;
"A novel silent posttranslational mechanism converts methionine to
aspartate in hemoglobin Bristol (beta 67[E11] Val-Met->Asp).";
Blood 88:341-348(1996).
[142]
VARIANT IRAQ-HALABJA VAL-11.
PubMed=10398311;
DOI=10.1002/(SICI)1096-8652(199907)61:3<187::AID-AJH5>3.0.CO;2-7;
Deutsch S., Darbellay R., Offord R.E., Frutiger A., Kister J.,
Wajcman H., Beris P.;
"Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain
silent variant in a family with multiple Hb disorders.";
Am. J. Hematol. 61:187-193(1999).
[143]
VARIANT VILLEJUIF ILE-124.
PubMed=11300351; DOI=10.1081/HEM-100103071;
Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C.,
Pucci P.;
"Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern
Italy.";
Hemoglobin 25:67-78(2001).
[144]
VARIANT TSUKUMI TYR-118.
PubMed=11300344; DOI=10.1081/HEM-100103076;
North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J.,
Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.;
"Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman.";
Hemoglobin 25:107-110(2001).
[145]
VARIANT CANTERBURY PHE-113.
PubMed=11939514; DOI=10.1081/HEM-120002942;
Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A.,
Ferguson M.M.;
"Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable
variant.";
Hemoglobin 26:67-69(2002).
[146]
VARIANT PYRGOS ASP-84, AND VARIANT B-THAL LYS-27.
PubMed=12144064; DOI=10.1081/HEM-120005459;
Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P.,
Srisomsap C., Svasti J., Fucharoen S.;
"Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E
[beta26(B8)Glu-->Lys] found in association with alpha-thalassemia.";
Hemoglobin 26:191-196(2002).
[147]
VARIANT SANTANDER ASP-35.
PubMed=12603091; DOI=10.1081/HEM-120016378;
Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E.,
Rodrigo E., Arias M.;
"Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable
variant found as a de novo mutation in a Spanish patient.";
Hemoglobin 27:31-35(2003).
[148]
VARIANT NANTES LEU-35, AND VARIANT VEXIN LEU-117.
PubMed=12908805; DOI=10.1081/HEM-120023384;
Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J.,
Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L.,
Galacteros F.;
"Two new hemoglobin variants with increased oxygen affinity: Hb Nantes
[beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu].";
Hemoglobin 27:191-199(2003).
[149]
VARIANT B-THAL LYS-27.
PubMed=15481886; DOI=10.1081/HEM-120040334;
Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.;
"The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta-
globin anomalies in the Lao Theung population of southern Laos.";
Hemoglobin 28:197-204(2004).
[150]
VARIANT BECKMAN ASP-136.
PubMed=19453576; DOI=10.1111/j.1751-553X.2009.01156.x;
Kim S.Y., Kim G.Y., Jo S.A., Lee E.H., Cho E.H., Hwang S.H., Lee E.Y.;
"A novel hemoglobin variant beta135(H13) Ala > Asp identified in an
asymptomatic Korean family by direct sequencing: suggesting a new
insight into Hb Beckman mutation.";
Int. J. Lab. Hematol. 32:E175-E178(2010).
[151]
VARIANT BECKMAN ASP-136, AND MASS SPECTROMETRY.
PubMed=26209877; DOI=10.1016/j.ab.2015.07.010;
Das R., Muralidharan M., Mitra G., Bhat V., Mathew B., Pal D.,
Ross C., Mandal A.K.;
"Mass spectrometry based characterization of Hb Beckman variant in a
falsely elevated HbA(1c) sample.";
Anal. Biochem. 489:53-58(2015).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues.
-!- FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin,
causing a decrease in blood pressure.
-!- FUNCTION: Spinorphin: functions as an endogenous inhibitor of
enkephalin-degrading enzymes such as DPP3, and as a selective
antagonist of the P2RX3 receptor which is involved in pain
signaling, these properties implicate it as a regulator of pain
and inflammation.
-!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
adult hemoglobin A (HbA). Heterotetramer of two zeta chains and
two beta chains in hemoglobin Portland-2, detected in fetuses and
neonates with homozygous alpha-thalassemia.
{ECO:0000269|PubMed:11747442, ECO:0000269|PubMed:24100324,
ECO:0000269|PubMed:6539334}.
-!- INTERACTION:
P69905:HBA2; NbExp=22; IntAct=EBI-715554, EBI-714680;
P02008:HBZ; NbExp=2; IntAct=EBI-715554, EBI-719843;
-!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:6539334}.
-!- PTM: Glucose reacts non-enzymatically with the N-terminus of the
beta chain to form a stable ketoamine linkage. This takes place
slowly and continuously throughout the 120-day life span of the
red blood cell. The rate of glycation is increased in patients
with diabetes mellitus.
-!- PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+)
and then transferred to Cys-94 to allow capture of O(2).
{ECO:0000269|PubMed:1520632, ECO:0000269|PubMed:8637569,
ECO:0000269|PubMed:9843411}.
-!- PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin
exposure. {ECO:0000269|PubMed:4531009}.
-!- MASS SPECTROMETRY: Mass=1310; Method=FAB; Range=33-42;
Evidence={ECO:0000269|PubMed:1575724};
-!- POLYMORPHISM: Genetic variations in HBB are involved in resistance
to malaria [MIM:611162]. Hemoglobin S (Hb S), which at
homozygosity is responsible for sickle cell anemia, is not
associated with any clinical abnormality when heterozygous. At
heterozygosity, Hb S confers an increase in protection from life-
threatening malaria. Additional variants conferring resistance
against severe malaria are hemoglobin C (Hb C) and hemoglobin E
(Hb E). {ECO:0000269|PubMed:11001883, ECO:0000269|PubMed:12149194,
ECO:0000269|PubMed:16001361}.
-!- DISEASE: Heinz body anemias (HEIBAN) [MIM:140700]: Form of non-
spherocytic hemolytic anemia of Dacie type 1. After splenectomy,
which has little benefit, basophilic inclusions called Heinz
bodies are demonstrable in the erythrocytes. Before splenectomy,
diffuse or punctate basophilia may be evident. Most of these cases
are probably instances of hemoglobinopathy. The hemoglobin
demonstrates heat lability. Heinz bodies are observed also with
the Ivemark syndrome (asplenia with cardiovascular anomalies) and
with glutathione peroxidase deficiency.
{ECO:0000269|PubMed:186485, ECO:0000269|PubMed:2599881,
ECO:0000269|PubMed:6259091, ECO:0000269|PubMed:8704193}. Note=The
disease may be caused by mutations affecting the gene represented
in this entry.
-!- DISEASE: Beta-thalassemia (B-THAL) [MIM:613985]: A form of
thalassemia. Thalassemias are common monogenic diseases occurring
mostly in Mediterranean and Southeast Asian populations. The
hallmark of beta-thalassemia is an imbalance in globin-chain
production in the adult HbA molecule. Absence of beta chain causes
beta(0)-thalassemia, while reduced amounts of detectable beta
globin causes beta(+)-thalassemia. In the severe forms of beta-
thalassemia, the excess alpha globin chains accumulate in the
developing erythroid precursors in the marrow. Their deposition
leads to a vast increase in erythroid apoptosis that in turn
causes ineffective erythropoiesis and severe microcytic
hypochromic anemia. Clinically, beta-thalassemia is divided into
thalassemia major which is transfusion dependent, thalassemia
intermedia (of intermediate severity), and thalassemia minor that
is asymptomatic. {ECO:0000269|PubMed:12144064,
ECO:0000269|PubMed:12149194, ECO:0000269|PubMed:15481886,
ECO:0000269|PubMed:2399911, ECO:0000269|PubMed:6166632,
ECO:0000269|PubMed:7693620}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Sickle cell anemia (SKCA) [MIM:603903]: Characterized by
abnormally shaped red cells resulting in chronic anemia and
periodic episodes of pain, serious infections and damage to vital
organs. Normal red blood cells are round and flexible and flow
easily through blood vessels, but in sickle cell anemia, the
abnormal hemoglobin (called Hb S) causes red blood cells to become
stiff. They are C-shaped and resembles a sickle. These stiffer red
blood cells can led to microvascular occlusion thus cutting off
the blood supply to nearby tissues. {ECO:0000269|PubMed:1195378,
ECO:0000269|PubMed:13464827, ECO:0000269|PubMed:16001361,
ECO:0000269|PubMed:24100324, ECO:0000269|Ref.10}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Beta-thalassemia, dominant, inclusion body type (B-
THALIB) [MIM:603902]: An autosomal dominant form of beta
thalassemia characterized by moderate anemia, lifelong jaundice,
cholelithiasis and splenomegaly, marked morphologic changes in the
red cells, erythroid hyperplasia of the bone marrow with increased
numbers of multinucleate red cell precursors, and the presence of
large inclusion bodies in the normoblasts, both in the marrow and
in the peripheral blood after splenectomy.
{ECO:0000269|PubMed:1971109}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: One molecule of 2,3-bisphosphoglycerate can bind to
two beta chains per hemoglobin tetramer.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-!- CAUTION: The modification form of Leu-142 is subject of
controversy and could be the artifactual result of sample
handling. {ECO:0000305|PubMed:1520632}.
-!- CAUTION: It is unclear if hemoglobin Beckman (Hb Beckman) is
defined by p.Ala136Glu or p.Ala136Asp. Hb Beckman has been
originally identified by reverse phase-HPLC and tandem mass
spectrometry, and has been reported as variant p.Ala136Glu
(Ref.139). Subsequently, variant p.Ala136Asp has been reported
based on HBB gene complete sequencing results (PubMed:19453576).
Variant p.Ala136Asp has also been detected by mass spectrometry
(PubMed:26209877). Although the name Hb Beckman is currently used
for variant p.Ala136Asp, it cannot be ruled out that Hb Beckman is
indeed variant p.Ala136Glu (PubMed:19453576).
{ECO:0000269|PubMed:19453576, ECO:0000269|PubMed:26209877,
ECO:0000269|Ref.139, ECO:0000303|PubMed:19453576}.
-!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
thalassemias;
URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBB";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBB";
-!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry;
URL="https://en.wikipedia.org/wiki/Hemoglobin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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-----------------------------------------------------------------------
EMBL; M25079; AAA35597.1; -; mRNA.
EMBL; V00499; CAA23758.1; -; Genomic_DNA.
EMBL; DQ126270; AAZ39745.1; -; Genomic_DNA.
EMBL; DQ126271; AAZ39746.1; -; Genomic_DNA.
EMBL; DQ126272; AAZ39747.1; -; Genomic_DNA.
EMBL; DQ126273; AAZ39748.1; -; Genomic_DNA.
EMBL; DQ126274; AAZ39749.1; -; Genomic_DNA.
EMBL; DQ126275; AAZ39750.1; -; Genomic_DNA.
EMBL; DQ126276; AAZ39751.1; -; Genomic_DNA.
EMBL; DQ126277; AAZ39752.1; -; Genomic_DNA.
EMBL; DQ126278; AAZ39753.1; -; Genomic_DNA.
EMBL; DQ126279; AAZ39754.1; -; Genomic_DNA.
EMBL; DQ126280; AAZ39755.1; -; Genomic_DNA.
EMBL; DQ126281; AAZ39756.1; -; Genomic_DNA.
EMBL; DQ126282; AAZ39757.1; -; Genomic_DNA.
EMBL; DQ126283; AAZ39758.1; -; Genomic_DNA.
EMBL; DQ126284; AAZ39759.1; -; Genomic_DNA.
EMBL; DQ126285; AAZ39760.1; -; Genomic_DNA.
EMBL; DQ126286; AAZ39761.1; -; Genomic_DNA.
EMBL; DQ126287; AAZ39762.1; -; Genomic_DNA.
EMBL; DQ126288; AAZ39763.1; -; Genomic_DNA.
EMBL; DQ126289; AAZ39764.1; -; Genomic_DNA.
EMBL; DQ126290; AAZ39765.1; -; Genomic_DNA.
EMBL; DQ126291; AAZ39766.1; -; Genomic_DNA.
EMBL; DQ126292; AAZ39767.1; -; Genomic_DNA.
EMBL; DQ126293; AAZ39768.1; -; Genomic_DNA.
EMBL; DQ126294; AAZ39769.1; -; Genomic_DNA.
EMBL; DQ126295; AAZ39770.1; -; Genomic_DNA.
EMBL; DQ126296; AAZ39771.1; -; Genomic_DNA.
EMBL; DQ126297; AAZ39772.1; -; Genomic_DNA.
EMBL; DQ126298; AAZ39773.1; -; Genomic_DNA.
EMBL; DQ126299; AAZ39774.1; -; Genomic_DNA.
EMBL; DQ126300; AAZ39775.1; -; Genomic_DNA.
EMBL; DQ126301; AAZ39776.1; -; Genomic_DNA.
EMBL; DQ126302; AAZ39777.1; -; Genomic_DNA.
EMBL; DQ126303; AAZ39778.1; -; Genomic_DNA.
EMBL; DQ126304; AAZ39779.1; -; Genomic_DNA.
EMBL; DQ126305; AAZ39780.1; -; Genomic_DNA.
EMBL; DQ126306; AAZ39781.1; -; Genomic_DNA.
EMBL; DQ126307; AAZ39782.1; -; Genomic_DNA.
EMBL; DQ126308; AAZ39783.1; -; Genomic_DNA.
EMBL; DQ126309; AAZ39784.1; -; Genomic_DNA.
EMBL; DQ126310; AAZ39785.1; -; Genomic_DNA.
EMBL; DQ126311; AAZ39786.1; -; Genomic_DNA.
EMBL; DQ126312; AAZ39787.1; -; Genomic_DNA.
EMBL; DQ126313; AAZ39788.1; -; Genomic_DNA.
EMBL; DQ126314; AAZ39789.1; -; Genomic_DNA.
EMBL; DQ126315; AAZ39790.1; -; Genomic_DNA.
EMBL; DQ126316; AAZ39791.1; -; Genomic_DNA.
EMBL; DQ126317; AAZ39792.1; -; Genomic_DNA.
EMBL; DQ126318; AAZ39793.1; -; Genomic_DNA.
EMBL; DQ126319; AAZ39794.1; -; Genomic_DNA.
EMBL; DQ126320; AAZ39795.1; -; Genomic_DNA.
EMBL; DQ126321; AAZ39796.1; -; Genomic_DNA.
EMBL; DQ126322; AAZ39797.1; -; Genomic_DNA.
EMBL; DQ126323; AAZ39798.1; -; Genomic_DNA.
EMBL; DQ126324; AAZ39799.1; -; Genomic_DNA.
EMBL; DQ126325; AAZ39800.1; -; Genomic_DNA.
EMBL; AF007546; AAB62944.1; -; Genomic_DNA.
EMBL; AF083883; AAL68978.1; -; Genomic_DNA.
EMBL; AF117710; AAD19696.1; -; mRNA.
EMBL; AF181989; AAF00489.1; -; mRNA.
EMBL; AF349114; AAK29639.1; -; mRNA.
EMBL; AF527577; AAM92001.1; -; Genomic_DNA.
EMBL; AY136510; AAN11320.1; -; mRNA.
EMBL; AY163866; AAN84548.1; -; Genomic_DNA.
EMBL; AY260740; AAP21062.1; -; Genomic_DNA.
EMBL; AY509193; AAR96398.1; -; mRNA.
EMBL; EF450778; ABO36678.1; -; Genomic_DNA.
EMBL; EU694432; ACD39349.1; -; mRNA.
EMBL; AK311825; BAG34767.1; -; mRNA.
EMBL; CR536530; CAG38767.1; -; mRNA.
EMBL; CR541913; CAG46711.1; -; mRNA.
EMBL; CH471064; EAW68806.1; -; Genomic_DNA.
EMBL; BC007075; AAH07075.1; -; mRNA.
EMBL; U01317; AAA16334.1; -; Genomic_DNA.
EMBL; V00497; CAA23756.1; -; mRNA.
EMBL; V00500; CAA23759.1; ALT_SEQ; mRNA.
EMBL; L26462; AAA21100.1; -; Genomic_DNA.
EMBL; L26463; AAA21101.1; -; Genomic_DNA.
EMBL; L26464; AAA21102.1; -; Genomic_DNA.
EMBL; L26465; AAA21103.1; -; Genomic_DNA.
EMBL; L26466; AAA21104.1; -; Genomic_DNA.
EMBL; L26467; AAA21105.1; -; Genomic_DNA.
EMBL; L26468; AAA21106.1; -; Genomic_DNA.
EMBL; L26469; AAA21107.1; -; Genomic_DNA.
EMBL; L26470; AAA21108.1; -; Genomic_DNA.
EMBL; L26471; AAA21109.1; -; Genomic_DNA.
EMBL; L26472; AAA21110.1; -; Genomic_DNA.
EMBL; L26473; AAA21111.1; -; Genomic_DNA.
EMBL; L26474; AAA21112.1; -; Genomic_DNA.
EMBL; L26475; AAA21113.1; -; Genomic_DNA.
EMBL; L26476; AAA21114.1; -; Genomic_DNA.
EMBL; L26477; AAA21115.1; -; Genomic_DNA.
EMBL; L26478; AAA21116.1; -; Genomic_DNA.
EMBL; L48213; AAA88063.1; -; Genomic_DNA.
EMBL; L48214; AAA88061.1; -; Genomic_DNA.
EMBL; L48215; AAA88059.1; -; Genomic_DNA.
EMBL; L48216; AAA88065.1; -; Genomic_DNA.
EMBL; L48217; AAA88067.1; -; Genomic_DNA.
EMBL; M36640; AAA52634.1; -; Genomic_DNA.
EMBL; M11428; AAA52633.1; -; mRNA.
EMBL; M25113; AAA35966.1; -; mRNA.
EMBL; L48932; AAA88054.1; -; Genomic_DNA.
CCDS; CCDS7753.1; -.
PIR; A53136; HBHU.
RefSeq; NP_000509.1; NM_000518.4.
UniGene; Hs.523443; -.
PDB; 1A00; X-ray; 2.00 A; B/D=3-147.
PDB; 1A01; X-ray; 1.80 A; B/D=3-147.
PDB; 1A0U; X-ray; 2.14 A; B/D=3-147.
PDB; 1A0Z; X-ray; 2.00 A; B/D=3-147.
PDB; 1A3N; X-ray; 1.80 A; B/D=2-147.
PDB; 1A3O; X-ray; 1.80 A; B/D=2-147.
PDB; 1ABW; X-ray; 2.00 A; B/D=3-147.
PDB; 1ABY; X-ray; 2.60 A; B/D=3-147.
PDB; 1AJ9; X-ray; 2.20 A; B=2-147.
PDB; 1B86; X-ray; 2.50 A; B/D=2-147.
PDB; 1BAB; X-ray; 1.50 A; B/D=2-147.
PDB; 1BBB; X-ray; 1.70 A; B/D=2-147.
PDB; 1BIJ; X-ray; 2.30 A; B/D=2-147.
PDB; 1BUW; X-ray; 1.90 A; B/D=2-147.
PDB; 1BZ0; X-ray; 1.50 A; B/D=2-147.
PDB; 1BZ1; X-ray; 1.59 A; B/D=2-147.
PDB; 1BZZ; X-ray; 1.59 A; B/D=2-147.
PDB; 1C7B; X-ray; 1.80 A; B/D=2-147.
PDB; 1C7C; X-ray; 1.80 A; B/D=2-147.
PDB; 1C7D; X-ray; 1.80 A; B/D=2-147.
PDB; 1CBL; X-ray; 1.80 A; A/B/C/D=2-147.
PDB; 1CBM; X-ray; 1.74 A; A/B/C/D=2-147.
PDB; 1CH4; X-ray; 2.50 A; A/B/C/D=2-146.
PDB; 1CLS; X-ray; 1.90 A; B/D=2-147.
PDB; 1CMY; X-ray; 3.00 A; B/D=2-147.
PDB; 1COH; X-ray; 2.90 A; B/D=2-147.
PDB; 1DKE; X-ray; 2.10 A; B/D=2-147.
PDB; 1DXT; X-ray; 1.70 A; B/D=1-147.
PDB; 1DXU; X-ray; 1.70 A; B/D=3-147.
PDB; 1DXV; X-ray; 1.70 A; B/D=3-147.
PDB; 1FN3; X-ray; 2.48 A; B/D=2-147.
PDB; 1G9V; X-ray; 1.85 A; B/D=2-147.
PDB; 1GBU; X-ray; 1.80 A; B/D=2-147.
PDB; 1GBV; X-ray; 2.00 A; B/D=2-147.
PDB; 1GLI; X-ray; 2.50 A; B/D=3-147.
PDB; 1GZX; X-ray; 2.10 A; B/D=2-147.
PDB; 1HAB; X-ray; 2.30 A; B/D=2-147.
PDB; 1HAC; X-ray; 2.60 A; B/D=2-147.
PDB; 1HBA; X-ray; 2.10 A; B/D=2-147.
PDB; 1HBB; X-ray; 1.90 A; B/D=2-147.
PDB; 1HBS; X-ray; 3.00 A; B/D/F/H=2-147.
PDB; 1HCO; X-ray; 2.70 A; B=2-147.
PDB; 1HDB; X-ray; 2.20 A; B/D=2-147.
PDB; 1HGA; X-ray; 2.10 A; B/D=2-147.
PDB; 1HGB; X-ray; 2.10 A; B/D=2-147.
PDB; 1HGC; X-ray; 2.10 A; B/D=2-147.
PDB; 1HHO; X-ray; 2.10 A; B=2-147.
PDB; 1IRD; X-ray; 1.25 A; B=2-147.
PDB; 1J3Y; X-ray; 1.55 A; B/D/F/H=2-147.
PDB; 1J3Z; X-ray; 1.60 A; B/D/F/H=2-147.
PDB; 1J40; X-ray; 1.45 A; B/D/F/H=2-147.
PDB; 1J41; X-ray; 1.45 A; B/D/F/H=2-147.
PDB; 1J7S; X-ray; 2.20 A; B/D=2-147.
PDB; 1J7W; X-ray; 2.00 A; B/D=2-147.
PDB; 1J7Y; X-ray; 1.70 A; B/D=2-147.
PDB; 1JY7; X-ray; 3.20 A; B/D/Q/S/V/X=2-147.
PDB; 1K0Y; X-ray; 1.87 A; B/D=2-147.
PDB; 1K1K; X-ray; 2.00 A; B=2-147.
PDB; 1KD2; X-ray; 1.87 A; B/D=2-147.
PDB; 1LFL; X-ray; 2.70 A; B/D/Q/S=2-147.
PDB; 1LFQ; X-ray; 2.60 A; B=2-147.
PDB; 1LFT; X-ray; 2.60 A; B=2-147.
PDB; 1LFV; X-ray; 2.80 A; B=2-147.
PDB; 1LFY; X-ray; 3.30 A; B=2-147.
PDB; 1LFZ; X-ray; 3.10 A; B=2-147.
PDB; 1LJW; X-ray; 2.16 A; B=2-147.
PDB; 1M9P; X-ray; 2.10 A; B/D=2-147.
PDB; 1MKO; X-ray; 2.18 A; B/D=2-147.
PDB; 1NEJ; X-ray; 2.10 A; B/D=2-147.
PDB; 1NIH; X-ray; 2.60 A; B/D=2-147.
PDB; 1NQP; X-ray; 1.73 A; B/D=2-147.
PDB; 1O1I; X-ray; 2.30 A; B=2-147.
PDB; 1O1J; X-ray; 1.90 A; B/D=2-147.
PDB; 1O1K; X-ray; 2.00 A; B/D=2-147.
PDB; 1O1L; X-ray; 1.80 A; B/D=2-147.
PDB; 1O1M; X-ray; 1.85 A; B/D=2-147.
PDB; 1O1N; X-ray; 1.80 A; B/D=2-147.
PDB; 1O1O; X-ray; 1.80 A; B/D=2-147.
PDB; 1O1P; X-ray; 1.80 A; B/D=2-147.
PDB; 1QI8; X-ray; 1.80 A; B/D=3-147.
PDB; 1QSH; X-ray; 1.70 A; B/D=2-147.
PDB; 1QSI; X-ray; 1.70 A; B/D=2-147.
PDB; 1QXD; X-ray; 2.25 A; B/D=2-147.
PDB; 1QXE; X-ray; 1.85 A; B/D=2-147.
PDB; 1R1X; X-ray; 2.15 A; B=2-147.
PDB; 1R1Y; X-ray; 1.80 A; B/D=2-147.
PDB; 1RPS; X-ray; 2.11 A; B/D=2-147.
PDB; 1RQ3; X-ray; 1.91 A; B/D=2-147.
PDB; 1RQ4; X-ray; 2.11 A; B/D=2-147.
PDB; 1RQA; X-ray; 2.11 A; B/D=2-147.
PDB; 1RVW; X-ray; 2.50 A; B=2-147.
PDB; 1SDK; X-ray; 1.80 A; B/D=2-147.
PDB; 1SDL; X-ray; 1.80 A; B/D=2-147.
PDB; 1THB; X-ray; 1.50 A; B/D=2-147.
PDB; 1UIW; X-ray; 1.50 A; B/D/F/H=2-147.
PDB; 1VWT; X-ray; 1.90 A; B/D=2-147.
PDB; 1XXT; X-ray; 1.91 A; B/D=2-147.
PDB; 1XY0; X-ray; 1.99 A; B/D=2-147.
PDB; 1XYE; X-ray; 2.13 A; B/D=2-147.
PDB; 1XZ2; X-ray; 1.90 A; B/D=2-147.
PDB; 1XZ4; X-ray; 2.00 A; B/D=2-147.
PDB; 1XZ5; X-ray; 2.11 A; B/D=2-147.
PDB; 1XZ7; X-ray; 1.90 A; B/D=2-147.
PDB; 1XZU; X-ray; 2.16 A; B/D=2-147.
PDB; 1XZV; X-ray; 2.11 A; B/D=2-147.
PDB; 1Y09; X-ray; 2.25 A; B/D=2-147.
PDB; 1Y0A; X-ray; 2.22 A; B/D=2-147.
PDB; 1Y0C; X-ray; 2.30 A; B/D=2-147.
PDB; 1Y0D; X-ray; 2.10 A; B/D=2-147.
PDB; 1Y0T; X-ray; 2.14 A; B/D=2-147.
PDB; 1Y0W; X-ray; 2.14 A; B/D=2-147.
PDB; 1Y22; X-ray; 2.16 A; B/D=2-147.
PDB; 1Y2Z; X-ray; 2.07 A; B/D=2-147.
PDB; 1Y31; X-ray; 2.13 A; B/D=2-147.
PDB; 1Y35; X-ray; 2.12 A; B/D=2-147.
PDB; 1Y45; X-ray; 2.00 A; B/D=2-147.
PDB; 1Y46; X-ray; 2.22 A; B/D=2-147.
PDB; 1Y4B; X-ray; 2.10 A; B/D=2-147.
PDB; 1Y4F; X-ray; 2.00 A; B/D=2-147.
PDB; 1Y4G; X-ray; 1.91 A; B/D=2-147.
PDB; 1Y4P; X-ray; 1.98 A; B/D=2-147.
PDB; 1Y4Q; X-ray; 2.11 A; B/D=2-147.
PDB; 1Y4R; X-ray; 2.22 A; B/D=2-147.
PDB; 1Y4V; X-ray; 1.84 A; B/D=2-147.
PDB; 1Y5F; X-ray; 2.14 A; B/D=2-147.
PDB; 1Y5J; X-ray; 2.03 A; B/D=2-147.
PDB; 1Y5K; X-ray; 2.20 A; B/D=2-147.
PDB; 1Y7C; X-ray; 2.10 A; B/D=2-147.
PDB; 1Y7D; X-ray; 1.90 A; B/D=2-147.
PDB; 1Y7G; X-ray; 2.10 A; B/D=2-147.
PDB; 1Y7Z; X-ray; 1.98 A; B/D=2-147.
PDB; 1Y83; X-ray; 1.90 A; B/D=2-145.
PDB; 1Y85; X-ray; 2.13 A; B/D=2-146.
PDB; 1Y8W; X-ray; 2.90 A; B/D=2-147.
PDB; 1YDZ; X-ray; 3.30 A; B/D=2-147.
PDB; 1YE0; X-ray; 2.50 A; B/D=2-147.
PDB; 1YE1; X-ray; 4.50 A; B/D=2-147.
PDB; 1YE2; X-ray; 1.80 A; B/D=2-147.
PDB; 1YEN; X-ray; 2.80 A; B/D=2-147.
PDB; 1YEO; X-ray; 2.22 A; B/D=2-147.
PDB; 1YEQ; X-ray; 2.75 A; B/D=2-147.
PDB; 1YEU; X-ray; 2.12 A; B/D=2-147.
PDB; 1YEV; X-ray; 2.11 A; B/D=2-147.
PDB; 1YFF; X-ray; 2.40 A; B/D/F/H=2-147.
PDB; 1YG5; X-ray; 2.70 A; B/D=2-147.
PDB; 1YGD; X-ray; 2.73 A; B/D=2-147.
PDB; 1YGF; X-ray; 2.70 A; B/D=2-147.
PDB; 1YH9; X-ray; 2.20 A; B/D=2-147.
PDB; 1YHE; X-ray; 2.10 A; B/D=2-147.
PDB; 1YHR; X-ray; 2.60 A; B/D=2-147.
PDB; 1YIE; X-ray; 2.40 A; B/D=2-147.
PDB; 1YIH; X-ray; 2.00 A; B/D=2-147.
PDB; 1YVQ; X-ray; 1.80 A; B/D=2-147.
PDB; 1YVT; X-ray; 1.80 A; B=2-147.
PDB; 1YZI; X-ray; 2.07 A; B=2-147.
PDB; 2D5Z; X-ray; 1.45 A; B/D=2-147.
PDB; 2D60; X-ray; 1.70 A; B/D=2-147.
PDB; 2DN1; X-ray; 1.25 A; B=2-147.
PDB; 2DN2; X-ray; 1.25 A; B/D=2-147.
PDB; 2DN3; X-ray; 1.25 A; B=2-147.
PDB; 2DXM; Neutron; 2.10 A; B/D=2-147.
PDB; 2H35; NMR; -; B/D=2-147.
PDB; 2HBC; X-ray; 2.10 A; B=2-147.
PDB; 2HBD; X-ray; 2.20 A; B=2-147.
PDB; 2HBE; X-ray; 2.00 A; B=2-147.
PDB; 2HBF; X-ray; 2.20 A; B=2-147.
PDB; 2HBS; X-ray; 2.05 A; B/D/F/H=2-147.
PDB; 2HCO; X-ray; 2.70 A; B=2-147.
PDB; 2HHB; X-ray; 1.74 A; B/D=2-147.
PDB; 2HHD; X-ray; 2.20 A; B/D=2-147.
PDB; 2HHE; X-ray; 2.20 A; B/D=4-147.
PDB; 2M6Z; NMR; -; B/D=2-147.
PDB; 2W6V; X-ray; 1.80 A; B/D=2-147.
PDB; 2W72; X-ray; 1.07 A; B/D=3-147.
PDB; 2YRS; X-ray; 2.30 A; B/D/K/O=2-147.
PDB; 3B75; X-ray; 2.30 A; B/D/F/H/T=2-147.
PDB; 3D17; X-ray; 2.80 A; B/D=2-147.
PDB; 3D7O; X-ray; 1.80 A; B=2-147.
PDB; 3DUT; X-ray; 1.55 A; B/D=2-147.
PDB; 3HHB; X-ray; 1.74 A; B/D=2-147.
PDB; 3HXN; X-ray; 2.00 A; B/D=2-147.
PDB; 3IC0; X-ray; 1.80 A; B/D=2-147.
PDB; 3IC2; X-ray; 2.40 A; B/D=2-147.
PDB; 3KMF; Neutron; 2.00 A; C/G=2-147.
PDB; 3NL7; X-ray; 1.80 A; B=2-147.
PDB; 3NMM; X-ray; 1.60 A; B/D=2-147.
PDB; 3ODQ; X-ray; 3.10 A; B/D=2-147.
PDB; 3ONZ; X-ray; 2.09 A; B=2-147.
PDB; 3OO4; X-ray; 1.90 A; B=2-147.
PDB; 3OO5; X-ray; 2.10 A; B=2-147.
PDB; 3P5Q; X-ray; 2.00 A; B=2-147.
PDB; 3QJB; X-ray; 1.80 A; B=2-147.
PDB; 3QJC; X-ray; 2.00 A; B=2-147.
PDB; 3QJD; X-ray; 1.56 A; B/D=2-147.
PDB; 3QJE; X-ray; 1.80 A; B/D=2-147.
PDB; 3R5I; X-ray; 2.20 A; B/D=2-147.
PDB; 3S65; X-ray; 1.80 A; B/D=2-147.
PDB; 3S66; X-ray; 1.40 A; B=2-147.
PDB; 3SZK; X-ray; 3.01 A; B/E=2-147.
PDB; 3W4U; X-ray; 1.95 A; B/D/F=2-147.
PDB; 3WCP; X-ray; 1.94 A; B/D=2-147.
PDB; 3WHM; X-ray; 1.85 A; B/F=2-147.
PDB; 4FC3; X-ray; 2.26 A; B=2-147.
PDB; 4HHB; X-ray; 1.74 A; B/D=2-147.
PDB; 4IJ2; X-ray; 4.24 A; B/D=2-147.
PDB; 4L7Y; X-ray; 1.80 A; B/D=2-147.
PDB; 4M4A; X-ray; 2.05 A; B=2-147.
PDB; 4M4B; X-ray; 2.00 A; B=2-147.
PDB; 4MQC; X-ray; 2.20 A; B=2-147.
PDB; 4MQG; X-ray; 1.68 A; B=2-147.
PDB; 4MQH; X-ray; 2.50 A; B=2-147.
PDB; 4MQI; X-ray; 1.92 A; B=2-147.
PDB; 4N7N; X-ray; 2.75 A; B/D/F/H/J/L=2-147.
PDB; 4N7O; X-ray; 2.50 A; B/D/F/H/J/L=2-147.
PDB; 4N7P; X-ray; 2.81 A; B/D/F/H/J/L=2-147.
PDB; 4N8T; X-ray; 1.90 A; B=2-147.
PDB; 4NI0; X-ray; 2.15 A; B=2-147.
PDB; 4NI1; X-ray; 1.90 A; B=2-147.
PDB; 4ROL; X-ray; 1.70 A; B/D=2-147.
PDB; 4ROM; X-ray; 1.90 A; B/D=2-147.
PDB; 4WJG; X-ray; 3.10 A; 1/B/G/L/Q/V=2-147.
PDB; 4X0L; X-ray; 2.05 A; B=2-147.
PDB; 4XS0; X-ray; 2.55 A; B=2-147.
PDB; 5E29; X-ray; 1.85 A; B/D=3-147.
PDB; 5E6E; X-ray; 1.76 A; B=2-147.
PDB; 5E83; X-ray; 1.80 A; B/D=2-147.
PDB; 5EE4; X-ray; 2.30 A; D/F=2-147.
PDB; 5HU6; X-ray; 2.90 A; B=3-143.
PDB; 5HY8; X-ray; 2.30 A; B/D/F/H/T=2-147.
PDB; 5JDO; X-ray; 3.20 A; D=3-147, F=3-146.
PDB; 5KDQ; X-ray; 2.15 A; B/D=2-147.
PDB; 5ME2; EM; 3.20 A; B/D=2-144.
PDB; 5NI1; EM; 3.20 A; B/D=2-147.
PDB; 5SW7; X-ray; 1.85 A; B=2-147.
PDB; 5U3I; X-ray; 1.95 A; B/D=2-147.
PDB; 5UCU; X-ray; 1.80 A; B=2-147.
PDB; 5UFJ; X-ray; 2.05 A; B/D=2-147.
PDB; 5URC; X-ray; 1.85 A; B/D=2-147.
PDB; 6HBW; X-ray; 2.00 A; B/D=2-147.
PDBsum; 1A00; -.
PDBsum; 1A01; -.
PDBsum; 1A0U; -.
PDBsum; 1A0Z; -.
PDBsum; 1A3N; -.
PDBsum; 1A3O; -.
PDBsum; 1ABW; -.
PDBsum; 1ABY; -.
PDBsum; 1AJ9; -.
PDBsum; 1B86; -.
PDBsum; 1BAB; -.
PDBsum; 1BBB; -.
PDBsum; 1BIJ; -.
PDBsum; 1BUW; -.
PDBsum; 1BZ0; -.
PDBsum; 1BZ1; -.
PDBsum; 1BZZ; -.
PDBsum; 1C7B; -.
PDBsum; 1C7C; -.
PDBsum; 1C7D; -.
PDBsum; 1CBL; -.
PDBsum; 1CBM; -.
PDBsum; 1CH4; -.
PDBsum; 1CLS; -.
PDBsum; 1CMY; -.
PDBsum; 1COH; -.
PDBsum; 1DKE; -.
PDBsum; 1DXT; -.
PDBsum; 1DXU; -.
PDBsum; 1DXV; -.
PDBsum; 1FN3; -.
PDBsum; 1G9V; -.
PDBsum; 1GBU; -.
PDBsum; 1GBV; -.
PDBsum; 1GLI; -.
PDBsum; 1GZX; -.
PDBsum; 1HAB; -.
PDBsum; 1HAC; -.
PDBsum; 1HBA; -.
PDBsum; 1HBB; -.
PDBsum; 1HBS; -.
PDBsum; 1HCO; -.
PDBsum; 1HDB; -.
PDBsum; 1HGA; -.
PDBsum; 1HGB; -.
PDBsum; 1HGC; -.
PDBsum; 1HHO; -.
PDBsum; 1IRD; -.
PDBsum; 1J3Y; -.
PDBsum; 1J3Z; -.
PDBsum; 1J40; -.
PDBsum; 1J41; -.
PDBsum; 1J7S; -.
PDBsum; 1J7W; -.
PDBsum; 1J7Y; -.
PDBsum; 1JY7; -.
PDBsum; 1K0Y; -.
PDBsum; 1K1K; -.
PDBsum; 1KD2; -.
PDBsum; 1LFL; -.
PDBsum; 1LFQ; -.
PDBsum; 1LFT; -.
PDBsum; 1LFV; -.
PDBsum; 1LFY; -.
PDBsum; 1LFZ; -.
PDBsum; 1LJW; -.
PDBsum; 1M9P; -.
PDBsum; 1MKO; -.
PDBsum; 1NEJ; -.
PDBsum; 1NIH; -.
PDBsum; 1NQP; -.
PDBsum; 1O1I; -.
PDBsum; 1O1J; -.
PDBsum; 1O1K; -.
PDBsum; 1O1L; -.
PDBsum; 1O1M; -.
PDBsum; 1O1N; -.
PDBsum; 1O1O; -.
PDBsum; 1O1P; -.
PDBsum; 1QI8; -.
PDBsum; 1QSH; -.
PDBsum; 1QSI; -.
PDBsum; 1QXD; -.
PDBsum; 1QXE; -.
PDBsum; 1R1X; -.
PDBsum; 1R1Y; -.
PDBsum; 1RPS; -.
PDBsum; 1RQ3; -.
PDBsum; 1RQ4; -.
PDBsum; 1RQA; -.
PDBsum; 1RVW; -.
PDBsum; 1SDK; -.
PDBsum; 1SDL; -.
PDBsum; 1THB; -.
PDBsum; 1UIW; -.
PDBsum; 1VWT; -.
PDBsum; 1XXT; -.
PDBsum; 1XY0; -.
PDBsum; 1XYE; -.
PDBsum; 1XZ2; -.
PDBsum; 1XZ4; -.
PDBsum; 1XZ5; -.
PDBsum; 1XZ7; -.
PDBsum; 1XZU; -.
PDBsum; 1XZV; -.
PDBsum; 1Y09; -.
PDBsum; 1Y0A; -.
PDBsum; 1Y0C; -.
PDBsum; 1Y0D; -.
PDBsum; 1Y0T; -.
PDBsum; 1Y0W; -.
PDBsum; 1Y22; -.
PDBsum; 1Y2Z; -.
PDBsum; 1Y31; -.
PDBsum; 1Y35; -.
PDBsum; 1Y45; -.
PDBsum; 1Y46; -.
PDBsum; 1Y4B; -.
PDBsum; 1Y4F; -.
PDBsum; 1Y4G; -.
PDBsum; 1Y4P; -.
PDBsum; 1Y4Q; -.
PDBsum; 1Y4R; -.
PDBsum; 1Y4V; -.
PDBsum; 1Y5F; -.
PDBsum; 1Y5J; -.
PDBsum; 1Y5K; -.
PDBsum; 1Y7C; -.
PDBsum; 1Y7D; -.
PDBsum; 1Y7G; -.
PDBsum; 1Y7Z; -.
PDBsum; 1Y83; -.
PDBsum; 1Y85; -.
PDBsum; 1Y8W; -.
PDBsum; 1YDZ; -.
PDBsum; 1YE0; -.
PDBsum; 1YE1; -.
PDBsum; 1YE2; -.
PDBsum; 1YEN; -.
PDBsum; 1YEO; -.
PDBsum; 1YEQ; -.
PDBsum; 1YEU; -.
PDBsum; 1YEV; -.
PDBsum; 1YFF; -.
PDBsum; 1YG5; -.
PDBsum; 1YGD; -.
PDBsum; 1YGF; -.
PDBsum; 1YH9; -.
PDBsum; 1YHE; -.
PDBsum; 1YHR; -.
PDBsum; 1YIE; -.
PDBsum; 1YIH; -.
PDBsum; 1YVQ; -.
PDBsum; 1YVT; -.
PDBsum; 1YZI; -.
PDBsum; 2D5Z; -.
PDBsum; 2D60; -.
PDBsum; 2DN1; -.
PDBsum; 2DN2; -.
PDBsum; 2DN3; -.
PDBsum; 2DXM; -.
PDBsum; 2H35; -.
PDBsum; 2HBC; -.
PDBsum; 2HBD; -.
PDBsum; 2HBE; -.
PDBsum; 2HBF; -.
PDBsum; 2HBS; -.
PDBsum; 2HCO; -.
PDBsum; 2HHB; -.
PDBsum; 2HHD; -.
PDBsum; 2HHE; -.
PDBsum; 2M6Z; -.
PDBsum; 2W6V; -.
PDBsum; 2W72; -.
PDBsum; 2YRS; -.
PDBsum; 3B75; -.
PDBsum; 3D17; -.
PDBsum; 3D7O; -.
PDBsum; 3DUT; -.
PDBsum; 3HHB; -.
PDBsum; 3HXN; -.
PDBsum; 3IC0; -.
PDBsum; 3IC2; -.
PDBsum; 3KMF; -.
PDBsum; 3NL7; -.
PDBsum; 3NMM; -.
PDBsum; 3ODQ; -.
PDBsum; 3ONZ; -.
PDBsum; 3OO4; -.
PDBsum; 3OO5; -.
PDBsum; 3P5Q; -.
PDBsum; 3QJB; -.
PDBsum; 3QJC; -.
PDBsum; 3QJD; -.
PDBsum; 3QJE; -.
PDBsum; 3R5I; -.
PDBsum; 3S65; -.
PDBsum; 3S66; -.
PDBsum; 3SZK; -.
PDBsum; 3W4U; -.
PDBsum; 3WCP; -.
PDBsum; 3WHM; -.
PDBsum; 4FC3; -.
PDBsum; 4HHB; -.
PDBsum; 4IJ2; -.
PDBsum; 4L7Y; -.
PDBsum; 4M4A; -.
PDBsum; 4M4B; -.
PDBsum; 4MQC; -.
PDBsum; 4MQG; -.
PDBsum; 4MQH; -.
PDBsum; 4MQI; -.
PDBsum; 4N7N; -.
PDBsum; 4N7O; -.
PDBsum; 4N7P; -.
PDBsum; 4N8T; -.
PDBsum; 4NI0; -.
PDBsum; 4NI1; -.
PDBsum; 4ROL; -.
PDBsum; 4ROM; -.
PDBsum; 4WJG; -.
PDBsum; 4X0L; -.
PDBsum; 4XS0; -.
PDBsum; 5E29; -.
PDBsum; 5E6E; -.
PDBsum; 5E83; -.
PDBsum; 5EE4; -.
PDBsum; 5HU6; -.
PDBsum; 5HY8; -.
PDBsum; 5JDO; -.
PDBsum; 5KDQ; -.
PDBsum; 5ME2; -.
PDBsum; 5NI1; -.
PDBsum; 5SW7; -.
PDBsum; 5U3I; -.
PDBsum; 5UCU; -.
PDBsum; 5UFJ; -.
PDBsum; 5URC; -.
PDBsum; 6HBW; -.
ProteinModelPortal; P68871; -.
SMR; P68871; -.
BioGrid; 109293; 61.
DIP; DIP-35526N; -.
IntAct; P68871; 8.
MINT; MINT-5000306; -.
STRING; 9606.ENSP00000333994; -.
ChEMBL; CHEMBL4331; -.
DrugBank; DB07427; 2-[(2-methoxy-5-methylphenoxy)methyl]pyridine.
DrugBank; DB07428; 4-[(5-methoxy-2-methylphenoxy)methyl]pyridine.
DrugBank; DB02126; 4-Carboxycinnamic Acid.
DrugBank; DB00893; Iron Dextran.
DrugBank; DB07645; SEBACIC ACID.
TCDB; 1.A.107.1.2; the pore-forming globin (globin) family.
iPTMnet; P68871; -.
PhosphoSitePlus; P68871; -.
BioMuta; HBB; -.
DMDM; 56749856; -.
REPRODUCTION-2DPAGE; IPI00654755; -.
REPRODUCTION-2DPAGE; P68871; -.
SWISS-2DPAGE; P68871; -.
UCD-2DPAGE; P68871; -.
EPD; P68871; -.
MaxQB; P68871; -.
PaxDb; P68871; -.
PeptideAtlas; P68871; -.
PRIDE; P68871; -.
TopDownProteomics; P68871; -.
DNASU; 3043; -.
Ensembl; ENST00000335295; ENSP00000333994; ENSG00000244734.
GeneID; 3043; -.
KEGG; hsa:3043; -.
UCSC; uc001mae.2; human.
CTD; 3043; -.
DisGeNET; 3043; -.
GeneCards; HBB; -.
GeneReviews; HBB; -.
HGNC; HGNC:4827; HBB.
HPA; CAB009526; -.
HPA; HPA043234; -.
MalaCards; HBB; -.
MIM; 140700; phenotype.
MIM; 141900; gene+phenotype.
MIM; 603902; phenotype.
MIM; 603903; phenotype.
MIM; 611162; phenotype.
MIM; 613985; phenotype.
neXtProt; NX_P68871; -.
OpenTargets; ENSG00000244734; -.
Orphanet; 330041; Autosomal dominant methemoglobinemia.
Orphanet; 231222; Beta-thalassemia intermedia.
Orphanet; 231214; Beta-thalassemia major.
Orphanet; 231237; Delta-beta-thalassemia.
Orphanet; 231226; Dominant beta-thalassemia.
Orphanet; 178330; Heinz body anemia.
Orphanet; 231242; Hemoglobin C - beta-thalassemia.
Orphanet; 2132; Hemoglobin C disease.
Orphanet; 90039; Hemoglobin D disease.
Orphanet; 231249; Hemoglobin E - beta-thalassemia.
Orphanet; 2133; Hemoglobin E disease.
Orphanet; 330032; Hemoglobin Lepore - beta-thalassemia.
Orphanet; 46532; Hereditary persistence of fetal hemoglobin - beta-thalassemia.
Orphanet; 251380; Hereditary persistence of fetal hemoglobin - sickle cell disease.
Orphanet; 251359; Sickle cell - beta-thalassemia disease.
Orphanet; 251365; Sickle cell - hemoglobin C disease.
Orphanet; 251370; Sickle cell - hemoglobin D disease.
Orphanet; 251375; Sickle cell - hemoglobin E disease.
Orphanet; 232; Sickle cell anemia.
PharmGKB; PA29202; -.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
GeneTree; ENSGT00760000119197; -.
HOVERGEN; HBG009709; -.
InParanoid; P68871; -.
KO; K13823; -.
OMA; WTRRFFE; -.
OrthoDB; EOG091G0R7W; -.
PhylomeDB; P68871; -.
TreeFam; TF333268; -.
Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; P68871; -.
ChiTaRS; HBB; human.
EvolutionaryTrace; P68871; -.
GeneWiki; HBB; -.
GenomeRNAi; 3043; -.
PMAP-CutDB; P68871; -.
PRO; PR:P68871; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000244734; -.
ExpressionAtlas; P68871; baseline and differential.
Genevisible; P68871; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL.
GO; GO:0005833; C:hemoglobin complex; IDA:BHF-UCL.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0030492; F:hemoglobin binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; IDA:UniProtKB.
GO; GO:0005344; F:oxygen transporter activity; NAS:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030185; P:nitric oxide transport; NAS:UniProtKB.
GO; GO:0015671; P:oxygen transport; TAS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IDA:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
GO; GO:0050880; P:regulation of blood vessel size; IEA:UniProtKB-KW.
GO; GO:0070293; P:renal absorption; IMP:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL.
CDD; cd08925; Hb-beta_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like.
InterPro; IPR002337; Haemoglobin_b.
Pfam; PF00042; Globin; 1.
PRINTS; PR00814; BETAHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Congenital dyserythropoietic anemia; Direct protein sequencing;
Disease mutation; Glycation; Glycoprotein; Heme;
Hereditary hemolytic anemia; Hypotensive agent; Iron; Metal-binding;
Oxygen transport; Phosphoprotein; Polymorphism; Pyruvate;
Reference proteome; S-nitrosylation; Transport; Vasoactive.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P02086,
ECO:0000269|PubMed:13872627}.
CHAIN 2 147 Hemoglobin subunit beta.
/FTId=PRO_0000052976.
PEPTIDE 33 42 LVV-hemorphin-7.
/FTId=PRO_0000296641.
PEPTIDE 33 39 Spinorphin.
/FTId=PRO_0000424226.
METAL 64 64 Iron (heme distal ligand).
METAL 93 93 Iron (heme proximal ligand).
BINDING 2 2 2,3-bisphosphoglycerate; via amino
nitrogen.
BINDING 3 3 2,3-bisphosphoglycerate.
BINDING 83 83 2,3-bisphosphoglycerate.
BINDING 144 144 2,3-bisphosphoglycerate.
SITE 60 60 Not glycated.
{ECO:0000269|PubMed:7358733}.
SITE 83 83 Not glycated.
{ECO:0000269|PubMed:7358733}.
SITE 96 96 Not glycated.
{ECO:0000269|PubMed:7358733}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000250|UniProtKB:P02086}.
MOD_RES 2 2 N-pyruvate 2-iminyl-valine; in Hb A1b.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 51 51 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000269|PubMed:4531009}.
MOD_RES 83 83 N6-acetyllysine.
{ECO:0000269|PubMed:4531009}.
MOD_RES 88 88 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 94 94 S-nitrosocysteine.
{ECO:0000269|PubMed:8637569,
ECO:0000269|PubMed:9843411}.
MOD_RES 145 145 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:4531009}.
CARBOHYD 2 2 N-linked (Glc) (glycation) valine; in Hb
A1c. {ECO:0000269|PubMed:635569}.
CARBOHYD 9 9 N-linked (Glc) (glycation) lysine.
CARBOHYD 18 18 N-linked (Glc) (glycation) lysine.
CARBOHYD 67 67 N-linked (Glc) (glycation) lysine.
CARBOHYD 121 121 N-linked (Glc) (glycation) lysine.
CARBOHYD 145 145 N-linked (Glc) (glycation) lysine;
alternate.
VARIANT 2 2 V -> A (in Raleigh; O(2) affinity down;
dbSNP:rs33949930).
/FTId=VAR_002856.
VARIANT 3 3 H -> L (in Graz; dbSNP:rs35906307).
{ECO:0000269|PubMed:1487420}.
/FTId=VAR_002857.
VARIANT 3 3 H -> Q (in Okayama; O(2) affinity up;
dbSNP:rs713040).
/FTId=VAR_002858.
VARIANT 3 3 H -> R (in Deer Lodge; O(2) affinity up;
dbSNP:rs33983205).
/FTId=VAR_002859.
VARIANT 3 3 H -> Y (in Fukuoka; dbSNP:rs35906307).
/FTId=VAR_002860.
VARIANT 6 6 P -> R (in Warwickshire;
dbSNP:rs34769005).
/FTId=VAR_002861.
VARIANT 7 7 E -> A (in G-Makassar; dbSNP:rs334).
/FTId=VAR_002862.
VARIANT 7 7 E -> K (in Hb C; confers resistance to
severe malaria; dbSNP:rs33930165).
{ECO:0000269|PubMed:11001883,
ECO:0000269|PubMed:16175509}.
/FTId=VAR_002864.
VARIANT 7 7 E -> Q (in Machida; dbSNP:rs33930165).
/FTId=VAR_002865.
VARIANT 7 7 E -> V (in SKCA; Hb S; at heterozygosity
confers resistance to malaria;
dbSNP:rs334).
{ECO:0000269|PubMed:13464827,
ECO:0000269|PubMed:16001361,
ECO:0000269|Ref.10}.
/FTId=VAR_002863.
VARIANT 8 8 E -> G (in G-San Jose; mildly unstable;
dbSNP:rs34948328).
/FTId=VAR_002866.
VARIANT 8 8 E -> K (in G-Siriraj; dbSNP:rs34948328).
/FTId=VAR_002867.
VARIANT 9 9 K -> E (in N-Timone; dbSNP:rs33932981).
{ECO:0000269|PubMed:2634671}.
/FTId=VAR_002868.
VARIANT 9 9 K -> Q (in J-Luhe; dbSNP:rs33926764).
/FTId=VAR_002869.
VARIANT 9 9 K -> T (in Rio Grande; dbSNP:rs33932981).
{ECO:0000269|PubMed:6857757}.
/FTId=VAR_002870.
VARIANT 10 10 S -> C (in Porto Alegre; O(2) affinity
up; dbSNP:rs33918131).
/FTId=VAR_002871.
VARIANT 11 11 A -> D (in Ankara; dbSNP:rs33947457).
{ECO:0000269|PubMed:4850241}.
/FTId=VAR_002872.
VARIANT 11 11 A -> V (in Iraq-Halabja;
dbSNP:rs33947457).
{ECO:0000269|PubMed:10398311}.
/FTId=VAR_025393.
VARIANT 12 12 V -> D (in Windsor; O(2) affinity up;
unstable; dbSNP:rs33974228).
{ECO:0000269|PubMed:2599880}.
/FTId=VAR_002873.
VARIANT 12 12 V -> I (in Hamilton; dbSNP:rs33974228).
/FTId=VAR_002874.
VARIANT 14 14 A -> D (in J-Lens; dbSNP:rs35203747).
/FTId=VAR_002875.
VARIANT 15 15 L -> P (in Saki; unstable;
dbSNP:rs33935445).
/FTId=VAR_002876.
VARIANT 15 15 L -> R (in Soegn; unstable;
dbSNP:rs33935445).
/FTId=VAR_002877.
VARIANT 16 16 W -> G (in Randwick; unstable;
dbSNP:rs33946157).
{ECO:0000269|PubMed:3384707}.
/FTId=VAR_002878.
VARIANT 16 16 W -> R (in Belfast; O(2) affinity up;
unstable; dbSNP:rs33946157).
/FTId=VAR_002879.
VARIANT 17 17 G -> D (in J-Baltimore/J-Trinidad/J-
Ireland/J-Georgia/N-New Haven;
dbSNP:rs33962676).
/FTId=VAR_002880.
VARIANT 17 17 G -> R (in D-Bushman; dbSNP:rs63751285).
/FTId=VAR_002881.
VARIANT 18 18 K -> E (in Nagasaki; dbSNP:rs33986703).
/FTId=VAR_002882.
VARIANT 18 18 K -> N (in J-Amiens; dbSNP:rs36006214).
/FTId=VAR_002883.
VARIANT 18 18 K -> Q (in Nikosia; dbSNP:rs33986703).
/FTId=VAR_002884.
VARIANT 19 19 V -> M (in Baden; slightly unstable;
dbSNP:rs35802118).
/FTId=VAR_002885.
VARIANT 20 20 N -> D (in Alamo; dbSNP:rs34866629).
/FTId=VAR_002886.
VARIANT 20 20 N -> K (in D-Ouleh RABAH;
dbSNP:rs63750840).
/FTId=VAR_002887.
VARIANT 20 20 N -> S (in Malay; dbSNP:rs33972047).
/FTId=VAR_002888.
VARIANT 21 21 V -> M (in Olympia; O(2) affinity up;
dbSNP:rs35890959).
/FTId=VAR_002889.
VARIANT 22 22 D -> G (in Connecticut; O(2) affinity
down; dbSNP:rs33977536).
/FTId=VAR_002890.
VARIANT 22 22 D -> H (in Karlskoga; dbSNP:rs33950093).
{ECO:0000269|PubMed:8330972}.
/FTId=VAR_002892.
VARIANT 22 22 D -> N (in Cocody; dbSNP:rs33950093).
/FTId=VAR_002891.
VARIANT 22 22 D -> Y (in Yusa; dbSNP:rs33950093).
/FTId=VAR_002893.
VARIANT 23 23 E -> A (in G-Coushatta/G-Saskatoon/G-
Taegu/Hsin Chu; dbSNP:rs33936254).
/FTId=VAR_002894.
VARIANT 23 23 E -> G (in G-Taipei; dbSNP:rs33936254).
/FTId=VAR_002895.
VARIANT 23 23 E -> K (in E-Saskatoon;
dbSNP:rs33959855).
/FTId=VAR_002896.
VARIANT 23 23 E -> Q (in D-Iran; dbSNP:rs33959855).
/FTId=VAR_002897.
VARIANT 23 23 E -> V (in D-Granada; dbSNP:rs33936254).
/FTId=VAR_002898.
VARIANT 24 24 V -> D (in Strasbourg; O(2) affinity up;
dbSNP:rs33945546).
/FTId=VAR_002899.
VARIANT 24 24 V -> F (in Palmerston North; O(2)
affinity up; unstable; dbSNP:rs33929459).
{ECO:0000269|PubMed:7161106}.
/FTId=VAR_002900.
VARIANT 24 24 V -> G (in Miyashiro; O(2) affinity up;
unstable; dbSNP:rs33945546).
{ECO:0000269|PubMed:7338468}.
/FTId=VAR_002901.
VARIANT 24 24 Missing (in Freiburg; dbSNP:rs34160180).
{ECO:0000269|PubMed:5919752}.
/FTId=VAR_069169.
VARIANT 25 25 G -> D (in Moscva; O(2) affinity down;
unstable; dbSNP:rs33968721).
/FTId=VAR_002902.
VARIANT 25 25 G -> R (in Riverdale-Bronx; O(2) affinity
up; unstable; dbSNP:rs33972975).
/FTId=VAR_002903.
VARIANT 25 25 G -> V (in Savannah; unstable;
dbSNP:rs33968721).
/FTId=VAR_002904.
VARIANT 26 26 G -> D (in J-Auckland; unstable; O(2)
affinity down; dbSNP:rs35474880).
{ECO:0000269|PubMed:3654265}.
/FTId=VAR_002905.
VARIANT 26 26 G -> R (in G-Taiwan Ami;
dbSNP:rs34404985).
/FTId=VAR_002906.
VARIANT 27 27 E -> K (in B-THAL; Hb E; confers
resistance to severe malaria;
dbSNP:rs33950507).
{ECO:0000269|PubMed:12144064,
ECO:0000269|PubMed:12149194,
ECO:0000269|PubMed:15481886,
ECO:0000269|PubMed:6166632}.
/FTId=VAR_002907.
VARIANT 27 27 E -> V (in Henri Mondor; slightly
unstable; dbSNP:rs33915112).
/FTId=VAR_002908.
VARIANT 28 28 A -> D (in Volga/Drenthe; unstable;
dbSNP:rs33954632).
/FTId=VAR_002909.
VARIANT 28 28 A -> S (in Knossos; dbSNP:rs35424040).
{ECO:0000269|PubMed:7173395}.
/FTId=VAR_002910.
VARIANT 28 28 A -> V (in Grange-blanche; O(2) affinity
up; dbSNP:rs33954632).
{ECO:0000269|PubMed:3666141}.
/FTId=VAR_002911.
VARIANT 29 29 L -> P (in Genova/Hyogo; unstable;
dbSNP:rs33916412).
/FTId=VAR_002912.
VARIANT 29 29 L -> Q (in St Louis; dbSNP:rs33916412).
{ECO:0000269|PubMed:186485}.
/FTId=VAR_035236.
VARIANT 30 30 G -> D (in Lufkin; unstable;
dbSNP:rs35685286).
/FTId=VAR_002913.
VARIANT 31 31 R -> S (in Tacoma; unstable;
dbSNP:rs1135071).
/FTId=VAR_002914.
VARIANT 32 32 L -> P (in Yokohama; unstable;
dbSNP:rs33920173).
{ECO:0000269|PubMed:7338469}.
/FTId=VAR_002915.
VARIANT 33 33 L -> R (in Castilla; unstable;
dbSNP:rs33948578).
/FTId=VAR_002916.
VARIANT 33 33 L -> V (in Muscat; slightly unstable;
dbSNP:rs34314652).
{ECO:0000269|PubMed:1517102}.
/FTId=VAR_002917.
VARIANT 35 35 V -> D (in Santander; unstable;
dbSNP:rs1135101).
{ECO:0000269|PubMed:12603091}.
/FTId=VAR_025394.
VARIANT 35 35 V -> F (in Pitie-Salpetriere; O(2)
affinity up; dbSNP:rs1141387).
/FTId=VAR_002918.
VARIANT 35 35 V -> L (in Nantes; increased oxygen
affinity; dbSNP:rs1141387).
{ECO:0000269|PubMed:12908805}.
/FTId=VAR_025395.
VARIANT 36 36 Y -> F (in Philly; O(2) affinity up;
unstable; dbSNP:rs35857380).
/FTId=VAR_002919.
VARIANT 37 37 P -> R (in Sunnybrook; dbSNP:rs33993004).
/FTId=VAR_002920.
VARIANT 37 37 P -> S (in North Chicago; O(2) affinity
up; dbSNP:rs33948615).
{ECO:0000269|PubMed:3937824}.
/FTId=VAR_002921.
VARIANT 37 37 P -> T (in Linkoping/Finlandia; O(2)
affinity up; dbSNP:rs33948615).
{ECO:0000269|PubMed:3691763}.
/FTId=VAR_002922.
VARIANT 38 38 W -> G (in Howick; dbSNP:rs33994623).
{ECO:0000269|PubMed:8144352}.
/FTId=VAR_002923.
VARIANT 38 38 W -> R (in Rothschild; O(2) affinity
down; dbSNP:rs33994623).
{ECO:0000269|PubMed:1567857}.
/FTId=VAR_002925.
VARIANT 38 38 W -> S (in Hirose; O(2) affinity up;
dbSNP:rs33991059).
/FTId=VAR_002924.
VARIANT 39 39 T -> N (in Hinwil; O(2) affinity up;
dbSNP:rs34703513).
{ECO:0000269|PubMed:8745430}.
/FTId=VAR_002926.
VARIANT 40 40 Q -> E (in Vaasa; unstable;
dbSNP:rs76728603).
/FTId=VAR_002927.
VARIANT 40 40 Q -> K (in Alabama; dbSNP:rs76728603).
{ECO:0000269|PubMed:1115799}.
/FTId=VAR_002928.
VARIANT 40 40 Q -> R (in Tianshui; dbSNP:rs35973315).
/FTId=VAR_002929.
VARIANT 42 42 F -> Y (in Mequon; dbSNP:rs33926796).
/FTId=VAR_002930.
VARIANT 42 42 Missing (in Bruxelles).
{ECO:0000269|PubMed:2599881}.
/FTId=VAR_035237.
VARIANT 43 43 F -> L (in Louisville; unstable;
dbSNP:rs33924146). {ECO:0000269|Ref.6}.
/FTId=VAR_002931.
VARIANT 43 43 F -> S (in Hammersmith;
dbSNP:rs34378160).
{ECO:0000269|PubMed:6259091}.
/FTId=VAR_035239.
VARIANT 43 43 Missing (in Bruxelles).
{ECO:0000269|PubMed:2599881}.
/FTId=VAR_035238.
VARIANT 44 44 E -> Q (in Hoshida/Chaya;
dbSNP:rs33922842).
/FTId=VAR_002932.
VARIANT 45 45 S -> C (in Mississippi;
dbSNP:rs34868397).
/FTId=VAR_002933.
VARIANT 46 46 F -> S (in Cheverly; unstable;
dbSNP:rs33978338).
/FTId=VAR_002934.
VARIANT 47 47 G -> E (in K-Ibadan; dbSNP:rs35303218).
/FTId=VAR_002935.
VARIANT 48 48 D -> A (in Avicenna; dbSNP:rs33980484).
/FTId=VAR_002936.
VARIANT 48 48 D -> G (in Gavello; dbSNP:rs33980484).
/FTId=VAR_002937.
VARIANT 48 48 D -> Y (in Maputo; dbSNP:rs33932070).
{ECO:0000269|PubMed:6629824}.
/FTId=VAR_002938.
VARIANT 49 49 L -> P (in Bab-Saadoum; slightly
unstable; dbSNP:rs33952850).
/FTId=VAR_002939.
VARIANT 50 50 S -> F (in Las Palmas; slightly unstable;
dbSNP:rs33960931).
{ECO:0000269|PubMed:3384708,
ECO:0000269|Ref.13}.
/FTId=VAR_002940.
VARIANT 51 51 T -> K (in Edmonton).
/FTId=VAR_002941.
VARIANT 52 52 P -> R (in Willamette; O(2) affinity up;
unstable; dbSNP:rs33969727).
/FTId=VAR_002942.
VARIANT 53 53 D -> A (in Ocho Rios; dbSNP:rs33919924).
/FTId=VAR_002943.
VARIANT 53 53 D -> H (in Summer Hill;
dbSNP:rs33961886).
/FTId=VAR_002944.
VARIANT 55 55 V -> D (in Jacksonville; O(2) affinity
up; unstable; dbSNP:rs34037627).
{ECO:0000269|PubMed:2101840}.
/FTId=VAR_002945.
VARIANT 56 56 M -> K (in Matera; unstable;
dbSNP:rs35094013).
{ECO:0000269|PubMed:2384314}.
/FTId=VAR_002946.
VARIANT 57 57 G -> R (in Hamadan; dbSNP:rs33935983).
/FTId=VAR_002947.
VARIANT 58 58 N -> K (in G-ferrara; unstable;
dbSNP:rs35278874).
/FTId=VAR_002948.
VARIANT 59 59 P -> R (in Dhofar/Yukuhashi;
dbSNP:rs33991472).
/FTId=VAR_002949.
VARIANT 60 60 K -> E (in I-High Wycombe;
dbSNP:rs33969400).
/FTId=VAR_002950.
VARIANT 61 61 V -> A (in Collingwood; unstable;
dbSNP:rs33931779).
/FTId=VAR_002951.
VARIANT 62 62 K -> E (in N-Seatlle; dbSNP:rs33995148).
/FTId=VAR_002952.
VARIANT 62 62 K -> M (in Bologna; O(2) affinity down;
dbSNP:rs34974709).
/FTId=VAR_002953.
VARIANT 62 62 K -> N (in Hikari; dbSNP:rs34446260).
/FTId=VAR_002954.
VARIANT 63 63 A -> D (in J-Europa; dbSNP:rs34151786).
{ECO:0000269|PubMed:8811317}.
/FTId=VAR_002955.
VARIANT 63 63 A -> P (in Duarte; unstable;
dbSNP:rs34933455).
/FTId=VAR_002956.
VARIANT 64 64 H -> Y (in M-Saskatoon; O(2) affinity up;
dbSNP:rs33922873).
{ECO:0000269|PubMed:13897827}.
/FTId=VAR_002957.
VARIANT 66 66 K -> M (in J-Antakya; dbSNP:rs33932548).
{ECO:0000269|PubMed:3707969}.
/FTId=VAR_002958.
VARIANT 66 66 K -> N (in J-Sicilia; dbSNP:rs35747961).
{ECO:0000269|PubMed:4852224}.
/FTId=VAR_002959.
VARIANT 66 66 K -> Q (in J-Cairo; dbSNP:rs35353749).
{ECO:0000269|PubMed:1247583}.
/FTId=VAR_002960.
VARIANT 67 67 K -> T (in Chico; O(2) affinity down;
dbSNP:rs35939489).
/FTId=VAR_002961.
VARIANT 68 68 V -> A (in Sydney; unstable;
dbSNP:rs33918343).
/FTId=VAR_002962.
VARIANT 68 68 V -> D (in Bristol).
{ECO:0000269|PubMed:8704193}.
/FTId=VAR_035240.
VARIANT 68 68 V -> G (in non-spherocytic haemolytic
anemia; Manukau; dbSNP:rs33918343).
{ECO:0000269|PubMed:8280608}.
/FTId=VAR_040060.
VARIANT 68 68 V -> M (in Alesha; unstable;
dbSNP:rs36008922).
{ECO:0000269|PubMed:8330974}.
/FTId=VAR_002963.
VARIANT 69 69 L -> H (in Brisbane; O(2) affinity up;
dbSNP:rs33972593).
{ECO:0000269|PubMed:6166590}.
/FTId=VAR_002964.
VARIANT 69 69 L -> P (in Mizuho; unstable;
dbSNP:rs33972593).
{ECO:0000269|PubMed:893142}.
/FTId=VAR_002965.
VARIANT 70 70 G -> D (in Rambam; dbSNP:rs34718174).
{ECO:0000269|PubMed:9761252}.
/FTId=VAR_002966.
VARIANT 70 70 G -> R (in Kenitra; dbSNP:rs33947415).
/FTId=VAR_002967.
VARIANT 70 70 G -> S (in City of Hope;
dbSNP:rs33947415).
{ECO:0000269|PubMed:6434492}.
/FTId=VAR_002968.
VARIANT 71 71 A -> D (in Seattle; O(2) affinity down;
unstable; dbSNP:rs33946401).
/FTId=VAR_002969.
VARIANT 72 72 F -> S (in Christchurch; unstable;
dbSNP:rs34362537).
/FTId=VAR_002970.
VARIANT 74 74 D -> G (in Tilburg; O(2) affinity down;
dbSNP:rs33967755).
/FTId=VAR_002971.
VARIANT 74 74 D -> V (in Mobile; O(2) affinity down;
dbSNP:rs33967755).
/FTId=VAR_002972.
VARIANT 74 74 D -> Y (in Vancouver; O(2) affinity down;
dbSNP:rs33945705).
/FTId=VAR_002973.
VARIANT 75 75 G -> R (in Aalborg; unstable;
dbSNP:rs33916541).
/FTId=VAR_002974.
VARIANT 75 75 G -> V (in Bushwick; unstable;
dbSNP:rs33976006).
/FTId=VAR_002975.
VARIANT 76 76 L -> P (in Atlanta; unstable;
dbSNP:rs33950542). {ECO:0000269|Ref.13}.
/FTId=VAR_002976.
VARIANT 76 76 L -> R (in Pasadena; O(2) affinity up;
unstable; dbSNP:rs33950542).
/FTId=VAR_002977.
VARIANT 77 77 A -> D (in J-Chicago; dbSNP:rs33985847).
/FTId=VAR_002978.
VARIANT 78 78 H -> D (in J-Iran; dbSNP:rs33991294).
/FTId=VAR_002979.
VARIANT 78 78 H -> R (in Costa Rica; dbSNP:rs33952543).
{ECO:0000269|PubMed:8641705}.
/FTId=VAR_002980.
VARIANT 78 78 H -> Y (in Fukuyama; dbSNP:rs33991294).
/FTId=VAR_002981.
VARIANT 79 79 L -> R (in Quin-hai; dbSNP:rs34870172).
{ECO:0000269|PubMed:6629822}.
/FTId=VAR_002982.
VARIANT 80 80 D -> Y (in Tampa; dbSNP:rs33990858).
/FTId=VAR_002983.
VARIANT 81 81 N -> K (in G-Szuhu/Gifu;
dbSNP:rs35890380).
/FTId=VAR_002984.
VARIANT 82 82 L -> H (in La Roche-sur-Yon; unstable and
O(2) affinity up; dbSNP:rs33936967).
{ECO:0000269|PubMed:1540659}.
/FTId=VAR_012663.
VARIANT 82 82 L -> R (in Baylor; unstable;
dbSNP:rs33936967).
/FTId=VAR_002985.
VARIANT 82 82 L -> V (in dbSNP:rs11549406).
/FTId=VAR_049273.
VARIANT 83 83 K -> M (in Helsinki; O(2) affinity up;
dbSNP:rs33987903).
{ECO:0000269|PubMed:826083}.
/FTId=VAR_002986.
VARIANT 83 83 K -> N (in Providence; dbSNP:rs33991993).
/FTId=VAR_012664.
VARIANT 84 84 G -> D (in Pyrgos; dbSNP:rs1803195).
{ECO:0000269|PubMed:12144064}.
/FTId=VAR_025396.
VARIANT 84 84 G -> R (in Muskegon; dbSNP:rs33930385).
/FTId=VAR_002987.
VARIANT 85 85 T -> I (in Kofu; dbSNP:rs35914488).
{ECO:0000269|PubMed:3744871}.
/FTId=VAR_002988.
VARIANT 87 87 A -> D (in Olomouc; O(2) affinity up;
dbSNP:rs35819837).
{ECO:0000269|PubMed:3623975}.
/FTId=VAR_002989.
VARIANT 88 88 T -> I (in Quebec-Chori;
dbSNP:rs33993568).
/FTId=VAR_002990.
VARIANT 88 88 T -> K (in D-Ibadan; dbSNP:rs33993568).
/FTId=VAR_002991.
VARIANT 88 88 T -> P (in Valletta; dbSNP:rs35553496).
/FTId=VAR_002992.
VARIANT 89 89 L -> P (in Santa Ana; unstable;
dbSNP:rs33940204).
/FTId=VAR_002993.
VARIANT 89 89 L -> R (in Boras; unstable;
dbSNP:rs33940204).
/FTId=VAR_002994.
VARIANT 90 90 S -> N (in Creteil; O(2) affinity up;
dbSNP:rs33917628).
/FTId=VAR_002995.
VARIANT 90 90 S -> R (in Vanderbilt; O(2) affinity up;
dbSNP:rs35351128).
/FTId=VAR_002996.
VARIANT 91 91 E -> D (in Pierre-Benite; O(2) affinity
up; dbSNP:rs35002698).
{ECO:0000269|PubMed:3384709}.
/FTId=VAR_002997.
VARIANT 91 91 E -> K (in Agenogi; O(2) affinity down;
dbSNP:rs33913712).
/FTId=VAR_002998.
VARIANT 92 92 L -> P (in Sabine; unstable;
dbSNP:rs33917785).
/FTId=VAR_002999.
VARIANT 92 92 L -> R (in Caribbean; O(2) affinity down;
unstable; dbSNP:rs33917785).
{ECO:0000269|PubMed:992050}.
/FTId=VAR_003000.
VARIANT 93 93 H -> D (in J-Altgelds Gardens; unstable;
dbSNP:rs33924775).
{ECO:0000269|PubMed:721609}.
/FTId=VAR_003001.
VARIANT 93 93 H -> N (in Isehara; unstable;
dbSNP:rs33924775).
{ECO:0000269|PubMed:1787097}.
/FTId=VAR_003002.
VARIANT 93 93 H -> P (in Newcastle and Duino;
associated with S-104 in Duino; unstable;
dbSNP:rs33974325).
{ECO:0000269|PubMed:1511986}.
/FTId=VAR_003003.
VARIANT 93 93 H -> Q (in Istambul; unstable;
dbSNP:rs34083951).
{ECO:0000269|PubMed:4639022}.
/FTId=VAR_003004.
VARIANT 94 94 C -> R (in Okazaki; O(2) affinity up;
unstable; dbSNP:rs33972927).
/FTId=VAR_003005.
VARIANT 95 95 D -> G (in Chandigarh; dbSNP:rs34579351).
/FTId=VAR_003006.
VARIANT 95 95 D -> H (in Barcelona; O(2) affinity up;
dbSNP:rs33959340).
/FTId=VAR_003007.
VARIANT 95 95 D -> N (in Bunbury; O(2) affinity up;
dbSNP:rs33959340).
{ECO:0000269|PubMed:6629823}.
/FTId=VAR_003008.
VARIANT 96 96 K -> M (in J-Cordoba; dbSNP:rs35204496).
/FTId=VAR_003009.
VARIANT 96 96 K -> N (in Detroit; dbSNP:rs36038739).
/FTId=VAR_003010.
VARIANT 97 97 L -> P (in Debrousse; unstable; O(2)
affinity up; dbSNP:rs36081208).
{ECO:0000269|PubMed:8602627}.
/FTId=VAR_003011.
VARIANT 97 97 L -> V (in Regina; O(2) affinity up;
dbSNP:rs34665886).
/FTId=VAR_003012.
VARIANT 98 98 H -> L (in Wood; O(2) affinity up;
dbSNP:rs33951978).
/FTId=VAR_003013.
VARIANT 98 98 H -> P (in Nagoya; O(2) affinity up;
unstable; dbSNP:rs33951978).
{ECO:0000269|PubMed:3838976}.
/FTId=VAR_003014.
VARIANT 98 98 H -> Q (in Malmoe; O(2) affinity up;
dbSNP:rs34515413).
/FTId=VAR_003015.
VARIANT 98 98 H -> Y (in Moriguchi; dbSNP:rs33950993).
/FTId=VAR_003016.
VARIANT 99 99 V -> G (in Nottingham; unstable;
dbSNP:rs33985510).
/FTId=VAR_003017.
VARIANT 100 100 D -> E (in Coimbra; O(2) affinity up;
dbSNP:rs34013622).
{ECO:0000269|PubMed:1814856}.
/FTId=VAR_003018.
VARIANT 101 101 P -> L (in Brigham; O(2) affinity up;
dbSNP:rs33965000).
/FTId=VAR_003019.
VARIANT 101 101 P -> R (in New Mexico; dbSNP:rs33965000).
/FTId=VAR_003020.
VARIANT 102 102 E -> D (in Potomac; O(2) affinity up;
dbSNP:rs35209591).
/FTId=VAR_003021.
VARIANT 102 102 E -> G (in Alberta; O(2) affinity up;
dbSNP:rs33937393).
/FTId=VAR_003022.
VARIANT 102 102 E -> K (in British Columbia; O(2)
affinity up; dbSNP:rs33966487).
/FTId=VAR_003023.
VARIANT 102 102 E -> Q (in Rush; unstable;
dbSNP:rs33966487).
{ECO:0000269|PubMed:4129558}.
/FTId=VAR_003024.
VARIANT 103 103 N -> S (in Beth Israel; O(2) affinity
down; unstable; dbSNP:rs33948057).
/FTId=VAR_003025.
VARIANT 103 103 N -> Y (in St Mande; O(2) affinity down;
dbSNP:rs33927739).
{ECO:0000269|PubMed:7238856}.
/FTId=VAR_003026.
VARIANT 104 104 F -> L (in Heathrow; O(2) affinity up;
dbSNP:rs35067717).
/FTId=VAR_003027.
VARIANT 105 105 R -> S (in Camperdown and Duino;
associated with P-92 in Duino; unstable;
dbSNP:rs33914944).
{ECO:0000269|PubMed:1138922,
ECO:0000269|PubMed:1511986}.
/FTId=VAR_003028.
VARIANT 105 105 R -> T (in Sherwood Forest;
dbSNP:rs33911434).
/FTId=VAR_003029.
VARIANT 108 108 G -> R (in Burke; O(2) affinity down;
unstable; dbSNP:rs35017910).
{ECO:0000269|PubMed:8401300}.
/FTId=VAR_003030.
VARIANT 109 109 N -> K (in Presbyterian; O(2) affinity
down; unstable; dbSNP:rs34933751).
{ECO:0000269|PubMed:668922}.
/FTId=VAR_003031.
VARIANT 110 110 V -> M (in San Diego; O(2) affinity up;
dbSNP:rs33969677).
/FTId=VAR_003032.
VARIANT 111 111 L -> P (in Showa-Yakushiji;
dbSNP:rs35256489).
/FTId=VAR_003033.
VARIANT 112 112 V -> A (in Stanmore; O(2) affinity down;
unstable; dbSNP:rs35871407).
{ECO:0000269|PubMed:1917537}.
/FTId=VAR_003034.
VARIANT 113 113 C -> F (in Canterbury; dbSNP:rs33932908).
{ECO:0000269|PubMed:11939514}.
/FTId=VAR_025397.
VARIANT 113 113 C -> R (in Indianapolis;
dbSNP:rs35849199).
{ECO:0000269|PubMed:429365,
ECO:0000269|Ref.5}.
/FTId=VAR_003035.
VARIANT 113 113 C -> Y (in Yahata; dbSNP:rs33932908).
{ECO:0000269|PubMed:1917530}.
/FTId=VAR_003036.
VARIANT 115 115 L -> M (in Zengcheng; dbSNP:rs33917394).
{ECO:0000269|PubMed:2079435}.
/FTId=VAR_010144.
VARIANT 115 115 L -> P (in B-THAL; Durham-N.C./Brescia;
dbSNP:rs36015961).
{ECO:0000269|PubMed:1301199,
ECO:0000269|PubMed:8111050,
ECO:0000269|Ref.7}.
/FTId=VAR_010145.
VARIANT 116 116 A -> D (in B-THAL; Hradec Kralove;
unstable; dbSNP:rs35485099).
{ECO:0000269|PubMed:7693620}.
/FTId=VAR_003037.
VARIANT 116 116 A -> P (in Madrid; unstable;
dbSNP:rs34945623).
/FTId=VAR_003038.
VARIANT 117 117 H -> L (in Vexin; increased oxygen
affinity; dbSNP:rs33978082).
{ECO:0000269|PubMed:12908805}.
/FTId=VAR_025398.
VARIANT 117 117 H -> Q (in Hafnia; dbSNP:rs35209776).
/FTId=VAR_003039.
VARIANT 118 118 H -> P (in Saitama; unstable;
dbSNP:rs33935673).
{ECO:0000269|PubMed:6687721}.
/FTId=VAR_003040.
VARIANT 118 118 H -> R (in P-Galveston;
dbSNP:rs33935673).
/FTId=VAR_003041.
VARIANT 118 118 H -> Y (in Tsukumi; dbSNP:rs33935527).
{ECO:0000269|PubMed:11300344}.
/FTId=VAR_025399.
VARIANT 120 120 G -> A (in Iowa; dbSNP:rs33947020).
/FTId=VAR_003042.
VARIANT 121 121 K -> E (in Hijiyama; dbSNP:rs33924134).
/FTId=VAR_003043.
VARIANT 121 121 K -> I (in Jianghua; dbSNP:rs34303736).
{ECO:0000269|PubMed:6618888}.
/FTId=VAR_003044.
VARIANT 121 121 K -> Q (in Takamatsu; dbSNP:rs33924134).
/FTId=VAR_003045.
VARIANT 122 122 E -> A (in D-Neath; dbSNP:rs33987957).
{ECO:0000269|PubMed:8330979}.
/FTId=VAR_003046.
VARIANT 122 122 E -> G (in St Francis; dbSNP:rs33987957).
/FTId=VAR_003047.
VARIANT 122 122 E -> K (in O-Arab; dbSNP:rs33946267).
/FTId=VAR_003049.
VARIANT 122 122 E -> Q (in D-Los Angeles/D-Punjab/D-
Portugal/D-Chicago/D-Oak Ridge;
dbSNP:rs33946267).
/FTId=VAR_003048.
VARIANT 122 122 E -> V (in D-Camperdown/Beograd;
dbSNP:rs33987957).
/FTId=VAR_003050.
VARIANT 124 124 T -> I (in Villejuif; asymptomatic
variant; dbSNP:rs33935383).
{ECO:0000269|PubMed:11300351}.
/FTId=VAR_003051.
VARIANT 125 125 P -> Q (in Ty Gard; O(2) affinity up;
dbSNP:rs33983276). {ECO:0000269|Ref.8}.
/FTId=VAR_003053.
VARIANT 125 125 P -> R (in Khartoum; unstable;
dbSNP:rs33983276).
/FTId=VAR_003052.
VARIANT 125 125 P -> S (in Tunis; dbSNP:rs35461710).
/FTId=VAR_003054.
VARIANT 127 127 V -> A (in Beirut; dbSNP:rs33925391).
/FTId=VAR_003055.
VARIANT 127 127 V -> E (in Hofu; unstable;
dbSNP:rs33925391).
/FTId=VAR_003057.
VARIANT 127 127 V -> G (in B-THAL; Dhonburi/Neapolis;
unstable; dbSNP:rs33925391).
{ECO:0000269|PubMed:2399911}.
/FTId=VAR_003056.
VARIANT 128 128 Q -> E (in Complutense;
dbSNP:rs33971634).
{ECO:0000269|PubMed:3707969}.
/FTId=VAR_003058.
VARIANT 128 128 Q -> K (in Brest; unstable;
dbSNP:rs33971634).
{ECO:0000269|PubMed:3384710}.
/FTId=VAR_003059.
VARIANT 129 129 A -> D (in J-Guantanamo; unstable;
dbSNP:rs33957286).
/FTId=VAR_003060.
VARIANT 130 130 A -> P (in Crete; O(2) affinity up;
unstable; dbSNP:rs35939430).
/FTId=VAR_003061.
VARIANT 130 130 A -> V (in La Desirade; O(2) affinity
down; unstable; dbSNP:rs111645889).
{ECO:0000269|PubMed:3557994}.
/FTId=VAR_003062.
VARIANT 131 131 Y -> D (in Wien; unstable;
dbSNP:rs35834416).
/FTId=VAR_003063.
VARIANT 131 131 Y -> S (in Nevers; dbSNP:rs33937535).
/FTId=VAR_003064.
VARIANT 132 132 Q -> E (in Camden/Tokuchi/Motown;
dbSNP:rs33910209).
/FTId=VAR_003065.
VARIANT 132 132 Q -> K (in Shelby/Leslie/Deaconess;
unstable; dbSNP:rs33910209).
{ECO:0000269|PubMed:6526653}.
/FTId=VAR_003066.
VARIANT 132 132 Q -> P (in Shangai; unstable;
dbSNP:rs33950778).
/FTId=VAR_003067.
VARIANT 132 132 Q -> R (in Sarrebourg; unstable;
dbSNP:rs33950778).
/FTId=VAR_003068.
VARIANT 133 133 K -> N (in Yamagata; O(2) affinity down;
dbSNP:rs33946775).
/FTId=VAR_003069.
VARIANT 133 133 K -> Q (in K-Woolwich; dbSNP:rs33953406).
/FTId=VAR_003070.
VARIANT 134 134 V -> L (in Extredemura;
dbSNP:rs34095019).
/FTId=VAR_003071.
VARIANT 135 135 V -> E (in North Shore-Caracas; unstable;
dbSNP:rs33966761).
{ECO:0000269|PubMed:891976}.
/FTId=VAR_003072.
VARIANT 136 136 A -> D (in Beckman; originally reported
as E-136; O(2) affinity down; unstable;
dbSNP:rs35669628).
{ECO:0000269|PubMed:19453576,
ECO:0000269|PubMed:26209877,
ECO:0000269|Ref.139}.
/FTId=VAR_003073.
VARIANT 136 136 A -> P (in Altdorf; O(2) affinity up;
unstable; dbSNP:rs35492035).
/FTId=VAR_003074.
VARIANT 137 137 G -> D (in Hope; O(2) affinity down;
unstable; dbSNP:rs33949486).
/FTId=VAR_003075.
VARIANT 139 139 A -> P (in Brockton; unstable;
dbSNP:rs33919821).
/FTId=VAR_003076.
VARIANT 140 140 N -> D (in Geelong; unstable;
dbSNP:rs33910475).
{ECO:0000269|PubMed:1917539}.
/FTId=VAR_003077.
VARIANT 140 140 N -> K (in Hinsdale; O(2) affinity down;
dbSNP:rs34240441).
{ECO:0000269|PubMed:2513289}.
/FTId=VAR_003078.
VARIANT 140 140 N -> S (in S-Wake; associated with V-6).
{ECO:0000269|Ref.10}.
/FTId=VAR_025335.
VARIANT 140 140 N -> Y (in Aurora; O(2) affinity up;
dbSNP:rs33910475).
{ECO:0000269|PubMed:8718692}.
/FTId=VAR_003079.
VARIANT 141 141 A -> D (in Himeji; unstable; O(2)
affinity down; dbSNP:rs33927093).
{ECO:0000269|PubMed:3754244}.
/FTId=VAR_003080.
VARIANT 141 141 A -> T (in St Jacques; O(2) affinity up;
dbSNP:rs34980264).
/FTId=VAR_003081.
VARIANT 141 141 A -> V (in Puttelange; polycythemia; O(2)
affinity up; dbSNP:rs33927093).
{ECO:0000269|PubMed:8522332}.
/FTId=VAR_003082.
VARIANT 142 142 L -> R (in Olmsted; unstable;
dbSNP:rs35854892).
/FTId=VAR_003083.
VARIANT 143 143 A -> D (in Ohio; O(2) affinity up;
dbSNP:rs33921821).
/FTId=VAR_003084.
VARIANT 144 144 H -> D (in Rancho Mirage;
dbSNP:rs33929415).
/FTId=VAR_003085.
VARIANT 144 144 H -> P (in Syracuse; O(2) affinity up;
dbSNP:rs33918338).
/FTId=VAR_003087.
VARIANT 144 144 H -> Q (in Little Rock; O(2) affinity up;
dbSNP:rs36020563).
/FTId=VAR_003086.
VARIANT 144 144 H -> R (in Abruzzo; O(2) affinity up;
dbSNP:rs33918338).
/FTId=VAR_003088.
VARIANT 145 145 K -> E (in Mito; O(2) affinity up;
dbSNP:rs33964352).
/FTId=VAR_003089.
VARIANT 146 146 Y -> C (in Rainier; O(2) affinity up;
dbSNP:rs35117167).
/FTId=VAR_003090.
VARIANT 146 146 Y -> H (in Bethesda; O(2) affinity up;
dbSNP:rs33949869).
/FTId=VAR_003091.
VARIANT 147 147 H -> D (in Hiroshima; O(2) affinity up;
dbSNP:rs33961444).
/FTId=VAR_003092.
VARIANT 147 147 H -> L (in Cowtown; O(2) affinity up;
dbSNP:rs33954264).
/FTId=VAR_003093.
VARIANT 147 147 H -> P (in York; O(2) affinity up;
dbSNP:rs33954264).
/FTId=VAR_003094.
VARIANT 147 147 H -> Q (in Kodaira; O(2) affinity up;
dbSNP:rs33985739).
{ECO:0000269|PubMed:1634367}.
/FTId=VAR_003095.
CONFLICT 26 26 Missing (in Ref. 15; ACD39349).
{ECO:0000305}.
CONFLICT 42 42 F -> L (in Ref. 13; AAR96398).
{ECO:0000305}.
HELIX 6 17 {ECO:0000244|PDB:2W72}.
HELIX 21 35 {ECO:0000244|PDB:2W72}.
HELIX 37 42 {ECO:0000244|PDB:2W72}.
HELIX 44 46 {ECO:0000244|PDB:1IRD}.
HELIX 52 57 {ECO:0000244|PDB:2W72}.
HELIX 59 75 {ECO:0000244|PDB:2W72}.
TURN 78 80 {ECO:0000244|PDB:1IRD}.
HELIX 82 95 {ECO:0000244|PDB:2W72}.
HELIX 102 119 {ECO:0000244|PDB:2W72}.
HELIX 120 122 {ECO:0000244|PDB:2W72}.
HELIX 125 143 {ECO:0000244|PDB:2W72}.
HELIX 144 146 {ECO:0000244|PDB:1IRD}.
SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64;
MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
KEFTPPVQAA YQKVVAGVAN ALAHKYH


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